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      "YEAR_KIN": 2006.0,
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "PMID_KIN": "16406408",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.026",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.027",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.027",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.030",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "PMID_KIN": "16406408",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.017",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "UniProt": "P11961",
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      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
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      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.018",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -1.58,
      "ln(ku)_H2O": -9.0,
      "dGKIN_H2O": 18.38,
      "mf": -1.27,
      "mu": 4.12,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.,",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205421",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -1.58,
      "ln(ku)_H2O": -9.0,
      "dGKIN_H2O": 18.38,
      "mf": -1.27,
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      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.,",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205421",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
      "UniProt": "P01053",
      "PDB_wild": "1coa",
      "MUTATED_CHAIN": "I",
      "PFAM": [
         "PF00280"
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      "CATH": [
         "1coaI00 (3.30.10.10)"
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      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.75,
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      "dGKIN_H2O": 39.84,
      "mf": -5.7,
      "mu": 4.2,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CI2",
      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
      "UniProt": "P01053",
      "PDB_wild": "1coa",
      "MUTATED_CHAIN": "I",
      "PFAM": [
         "PF00280"
      ],
      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.75,
      "ln(ku)_H2O": -10.33,
      "dGKIN_H2O": 39.84,
      "mf": -5.7,
      "mu": 4.2,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "HEPES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.3,
      "ln(ku)_H2O": -1.72,
      "dGKIN_H2O": 19.87,
      "mf": -7.03,
      "mu": 1.38,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "HEPES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.3,
      "ln(ku)_H2O": -1.72,
      "dGKIN_H2O": 19.87,
      "mf": -7.03,
      "mu": 1.38,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.8,
      "ln(ku)_H2O": -0.42,
      "dGKIN_H2O": 17.89,
      "mf": -3.12,
      "mu": 1.12,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.8,
      "ln(ku)_H2O": -0.42,
      "dGKIN_H2O": 17.89,
      "mf": -3.12,
      "mu": 1.12,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Im9*",
      "SOURCE": "Escherichia coli",
      "LENGTH": 86.0,
      "UniProt": "P13479",
      "PDB_wild": "1imq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01320"
      ],
      "CATH": [
         "1imqA00 (1.10.1200.20)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.33,
      "ln(ku)_H2O": -1.87,
      "dGKIN_H2O": 22.79,
      "mf": -4.53,
      "mu": 0.26,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Im9*",
      "SOURCE": "Escherichia coli",
      "LENGTH": 86.0,
      "UniProt": "P13479",
      "PDB_wild": "1imq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01320"
      ],
      "CATH": [
         "1imqA00 (1.10.1200.20)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.33,
      "ln(ku)_H2O": -1.87,
      "dGKIN_H2O": 22.79,
      "mf": -4.53,
      "mu": 0.26,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.36,
      "ln(ku)_H2O": -2.77,
      "dGKIN_H2O": 27.58,
      "mf": -3.39,
      "mu": 1.03,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.36,
      "ln(ku)_H2O": -2.77,
      "dGKIN_H2O": 27.58,
      "mf": -3.39,
      "mu": 1.03,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.1,
      "ln(ku)_H2O": -3.25,
      "dGKIN_H2O": 18.21,
      "mf": -6.38,
      "mu": 2.08,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.1,
      "ln(ku)_H2O": -3.25,
      "dGKIN_H2O": 18.21,
      "mf": -6.38,
      "mu": 2.08,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 151.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.88,
      "ln(ku)_H2O": -4.34,
      "dGKIN_H2O": 22.84,
      "mf": -4.92,
      "mu": 1.68,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 151.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.88,
      "ln(ku)_H2O": -4.34,
      "dGKIN_H2O": 22.84,
      "mf": -4.92,
      "mu": 1.68,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "HEPES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.96,
      "ln(ku)_H2O": -3.86,
      "dGKIN_H2O": 26.81,
      "mf": -9.74,
      "mu": 4.8,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "HEPES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.96,
      "ln(ku)_H2O": -3.86,
      "dGKIN_H2O": 26.81,
      "mf": -9.74,
      "mu": 4.8,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "WT(F653W)",
      "MUTATION_PDB": "WT(F45W)",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.33,
      "ln(ku)_H2O": -6.84,
      "dGKIN_H2O": 35.11,
      "mf": -5.66,
      "mu": 3.43,
      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "WT(F653W)",
      "MUTATION_PDB": "WT(F45W)",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.33,
      "ln(ku)_H2O": -6.84,
      "dGKIN_H2O": 35.11,
      "mf": -5.66,
      "mu": 3.43,
      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.05,
      "ln(ku)_H2O": -4.83,
      "dGKIN_H2O": 14.57,
      "mf": -2.27,
      "mu": 0.55,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.05,
      "ln(ku)_H2O": -4.83,
      "dGKIN_H2O": 14.57,
      "mf": -2.27,
      "mu": 0.55,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Chemotaxis protein CheW",
      "SOURCE": "Thermotoga maritima",
      "LENGTH": 143.0,
      "UniProt": "Q56311",
      "PDB_wild": "1k0s",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01584"
      ],
      "CATH": [
         "1k0sA01 (2.30.30.40)",
         "1k0sA02 (2.40.50.180)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 7.44,
      "ln(ku)_H2O": -12.05,
      "dGKIN_H2O": 48.29,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Chemotaxis protein CheW",
      "SOURCE": "Thermotoga maritima",
      "LENGTH": 143.0,
      "UniProt": "Q56311",
      "PDB_wild": "1k0s",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01584"
      ],
      "CATH": [
         "1k0sA01 (2.30.30.40)",
         "1k0sA02 (2.40.50.180)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 7.44,
      "ln(ku)_H2O": -12.05,
      "dGKIN_H2O": 48.29,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "internalin B (SH3-like domain of virulence protein internalin B)",
      "SOURCE": "Listeria monocytogenes",
      "LENGTH": 71.0,
      "UniProt": "P0DQD3",
      "PDB_wild": "1m9s",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF13457"
      ],
      "CATH": [
         "1m9sA03 (2.30.30.170)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.98,
      "ln(ku)_H2O": -1.66,
      "dGKIN_H2O": 13.99,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "internalin B (SH3-like domain of virulence protein internalin B)",
      "SOURCE": "Listeria monocytogenes",
      "LENGTH": 71.0,
      "UniProt": "P0DQD3",
      "PDB_wild": "1m9s",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF13457"
      ],
      "CATH": [
         "1m9sA03 (2.30.30.170)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.98,
      "ln(ku)_H2O": -1.66,
      "dGKIN_H2O": 13.99,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Actin binding protein ABP1 SH3 domain",
      "SOURCE": "Saccharomyces cerevisiae",
      "LENGTH": 58.0,
      "UniProt": "P15891",
      "PDB_wild": "1jo8",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1jo8A00 (2.30.30.40)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 2.47,
      "ln(ku)_H2O": -2.72,
      "dGKIN_H2O": 10.22,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Actin binding protein ABP1 SH3 domain",
      "SOURCE": "Saccharomyces cerevisiae",
      "LENGTH": 58.0,
      "UniProt": "P15891",
      "PDB_wild": "1jo8",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1jo8A00 (2.30.30.40)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 2.47,
      "ln(ku)_H2O": -2.72,
      "dGKIN_H2O": 10.22,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Repressor protein cI",
      "SOURCE": "Escherichia phage lambda",
      "LENGTH": 78.0,
      "UniProt": "P03034",
      "PDB_wild": "3kz3",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01381"
      ],
      "CATH": [
         "3kz3A00 (1.10.260.40)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 10.38,
      "ln(ku)_H2O": 3.21,
      "dGKIN_H2O": 17.76,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Repressor protein cI",
      "SOURCE": "Escherichia phage lambda",
      "LENGTH": 78.0,
      "UniProt": "P03034",
      "PDB_wild": "3kz3",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01381"
      ],
      "CATH": [
         "3kz3A00 (1.10.260.40)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 10.38,
      "ln(ku)_H2O": 3.21,
      "dGKIN_H2O": 17.76,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "E3BD (F166W)",
      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
      "LENGTH": 45.0,
      "UniProt": "P11961",
      "PDB_wild": "1w4e",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02817"
      ],
      "CATH": [
         "1w4eA00 (4.10.320.10)"
      ],
      "EC_NUMBER": "2.3.1.12",
      "MUTATION_UNIPROT": "A131G",
      "MUTATION_PDB": "A131G",
      "SEC_STR": "Beta",
      "RSA": "14.2",
      "T": 25.0,
      "pH": 5.5,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "T-jump or stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.79,
      "dln(kf)_H2O": -0.44,
      "ln(ku)_H2O": 6.82,
      "dln(ku)_H2O": 3.82,
      "mf": -2.05,
      "mu": 0.42,
      "BACKGROUND_MUT_UNIPROT": [
         "F166W"
      ],
      "AUTHOR_KIN": "Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.",
      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.019",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "E3BD (F166W)",
      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
      "LENGTH": 45.0,
      "UniProt": "P11961",
      "PDB_wild": "1w4e",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02817"
      ],
      "CATH": [
         "1w4eA00 (4.10.320.10)"
      ],
      "EC_NUMBER": "2.3.1.12",
      "MUTATION_UNIPROT": "A131G",
      "MUTATION_PDB": "A131G",
      "SEC_STR": "Beta",
      "RSA": "14.2",
      "T": 25.0,
      "pH": 5.5,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "T-jump or stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.79,
      "dln(kf)_H2O": -0.44,
      "ln(ku)_H2O": 6.82,
      "dln(ku)_H2O": 3.82,
      "mf": -2.05,
      "mu": 0.42,
      "BACKGROUND_MUT_UNIPROT": [
         "F166W"
      ],
      "AUTHOR_KIN": "Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.",
      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.019",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "E3BD (F166W)",
      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
      "LENGTH": 45.0,
      "UniProt": "P11961",
      "PDB_wild": "1w4e",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02817"
      ],
      "CATH": [
         "1w4eA00 (4.10.320.10)"
      ],
      "EC_NUMBER": "2.3.1.12",
      "MUTATION_UNIPROT": "V135A",
      "MUTATION_PDB": "V135A",
      "SEC_STR": "Helix",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 5.5,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "T-jump or stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.93,
      "dln(kf)_H2O": -0.3,
      "ln(ku)_H2O": 6.51,
      "dln(ku)_H2O": 3.51,
      "mf": -1.92,
      "mu": 0.71,
      "BACKGROUND_MUT_UNIPROT": [
         "F166W"
      ],
      "AUTHOR_KIN": "Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.",
      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.020",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "E3BD (F166W)",
      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
      "LENGTH": 45.0,
      "UniProt": "P11961",
      "PDB_wild": "1w4e",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02817"
      ],
      "CATH": [
         "1w4eA00 (4.10.320.10)"
      ],
      "EC_NUMBER": "2.3.1.12",
      "MUTATION_UNIPROT": "V135A",
      "MUTATION_PDB": "V135A",
      "SEC_STR": "Helix",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 5.5,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "T-jump or stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.93,
      "dln(kf)_H2O": -0.3,
      "ln(ku)_H2O": 6.51,
      "dln(ku)_H2O": 3.51,
      "mf": -1.92,
      "mu": 0.71,
      "BACKGROUND_MUT_UNIPROT": [
         "F166W"
      ],
      "AUTHOR_KIN": "Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.",
      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.020",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "E3BD (F166W)",
      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
      "LENGTH": 45.0,
      "UniProt": "P11961",
      "PDB_wild": "1w4e",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02817"
      ],
      "CATH": [
         "1w4eA00 (4.10.320.10)"
      ],
      "EC_NUMBER": "2.3.1.12",
      "MUTATION_UNIPROT": "Y138F",
      "MUTATION_PDB": "Y138F",
      "SEC_STR": "Helix",
      "RSA": "18.9",
      "T": 25.0,
      "pH": 5.5,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "T-jump or stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.45,
      "dln(kf)_H2O": -0.78,
      "ln(ku)_H2O": 6.15,
      "dln(ku)_H2O": 3.15,
      "mf": -1.92,
      "mu": 1.05,
      "BACKGROUND_MUT_UNIPROT": [
         "F166W"
      ],
      "AUTHOR_KIN": "Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.",
      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.021",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "E3BD (F166W)",
      "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)",
      "LENGTH": 45.0,
      "UniProt": "P11961",
      "PDB_wild": "1w4e",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02817"
      ],
      "CATH": [
         "1w4eA00 (4.10.320.10)"
      ],
      "EC_NUMBER": "2.3.1.12",
      "MUTATION_UNIPROT": "Y138F",
      "MUTATION_PDB": "Y138F",
      "SEC_STR": "Helix",
      "RSA": "18.9",
      "T": 25.0,
      "pH": 5.5,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "T-jump or stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.45,
      "dln(kf)_H2O": -0.78,
      "ln(ku)_H2O": 6.15,
      "dln(ku)_H2O": 3.15,
      "mf": -1.92,
      "mu": 1.05,
      "BACKGROUND_MUT_UNIPROT": [
         "F166W"
      ],
      "AUTHOR_KIN": "Ferguson, N.,  Sharpe, T.D., Johnson, C.M., Fersht, A.R.",
      "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. Journal of molecular biology. https://doi.org/10.1016/j.jmb.2005.12.021",
      "YEAR_KIN": 2006.0,
      "PMID_KIN": "16406408",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "L107A",
      "MUTATION_PDB": "L106A",
      "SEC_STR": "Beta",
      "RSA": "20.7",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.44,
      "dln(kf)_H2O": -1.32,
      "ln(ku)_H2O": -5.86,
      "dln(ku)_H2O": 2.6,
      "mu": 2.18,
      "PhiF_H2O": 0.34,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205449",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "L107A",
      "MUTATION_PDB": "L106A",
      "SEC_STR": "Beta",
      "RSA": "20.7",
      "T": 25.0,
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      "ln(ku)_H2O": -5.29,
      "dln(ku)_H2O": 3.17,
      "mu": 2.35,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205438",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "V64A",
      "MUTATION_PDB": "V63A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -1.56,
      "dln(kf)_H2O": -2.44,
      "ln(ku)_H2O": -5.88,
      "dln(ku)_H2O": 2.58,
      "mu": 2.16,
      "PhiF_H2O": 0.49,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205439",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
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      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "V64A",
      "MUTATION_PDB": "V63A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -1.56,
      "dln(kf)_H2O": -2.44,
      "ln(ku)_H2O": -5.88,
      "dln(ku)_H2O": 2.58,
      "mu": 2.16,
      "PhiF_H2O": 0.49,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205439",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "T76A",
      "MUTATION_PDB": "T75A",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.65,
      "dln(kf)_H2O": -1.53,
      "ln(ku)_H2O": -5.51,
      "dln(ku)_H2O": 2.95,
      "mu": 2.5,
      "PhiF_H2O": 0.34,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205440",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "T76A",
      "MUTATION_PDB": "T75A",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.65,
      "dln(kf)_H2O": -1.53,
      "ln(ku)_H2O": -5.51,
      "dln(ku)_H2O": 2.95,
      "mu": 2.5,
      "PhiF_H2O": 0.34,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205440",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "L23",
      "SOURCE": "Thermus thermophilus",
      "LENGTH": 96.0,
      "UniProt": "Q9RA57",
      "PDB_wild": "1n88",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00276"
      ],
      "CATH": [
         "1n88A00 (3.30.70.330)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.02,
      "ln(ku)_H2O": -3.88,
      "dGKIN_H2O": 14.62,
      "mf": -3.46,
      "mu": 1.17,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205420",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "L23",
      "SOURCE": "Thermus thermophilus",
      "LENGTH": 96.0,
      "UniProt": "Q9RA57",
      "PDB_wild": "1n88",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00276"
      ],
      "CATH": [
         "1n88A00 (3.30.70.330)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.02,
      "ln(ku)_H2O": -3.88,
      "dGKIN_H2O": 14.62,
      "mf": -3.46,
      "mu": 1.17,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205420",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "NTL9",
      "SOURCE": "Geobacillus stearothermophilus",
      "LENGTH": 149.0,
      "UniProt": "P02417",
      "PDB_wild": "1div",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01281",
         "PF03948"
      ],
      "CATH": [
         "1divA01 (3.40.5.10)",
         "1divA02 (3.10.430.100)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.55,
      "ln(ku)_H2O": 0.08,
      "dGKIN_H2O": 16.03,
      "mf": -1.84,
      "mu": 0.71,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "NTL9",
      "SOURCE": "Geobacillus stearothermophilus",
      "LENGTH": 149.0,
      "UniProt": "P02417",
      "PDB_wild": "1div",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01281",
         "PF03948"
      ],
      "CATH": [
         "1divA01 (3.40.5.10)",
         "1divA02 (3.10.430.100)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.55,
      "ln(ku)_H2O": 0.08,
      "dGKIN_H2O": 16.03,
      "mf": -1.84,
      "mu": 0.71,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Src SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 64.0,
      "UniProt": "P00523",
      "PDB_wild": "1rlq",
      "MUTATED_CHAIN": "C",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1rlqC00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.36,
      "ln(ku)_H2O": -1.27,
      "dGKIN_H2O": 13.95,
      "mf": -4.19,
      "mu": 1.7,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Src SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 64.0,
      "UniProt": "P00523",
      "PDB_wild": "1rlq",
      "MUTATED_CHAIN": "C",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1rlqC00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.36,
      "ln(ku)_H2O": -1.27,
      "dGKIN_H2O": 13.95,
      "mf": -4.19,
      "mu": 1.7,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "L653A",
      "MUTATION_PDB": "L68A",
      "SEC_STR": "Helix",
      "RSA": "5.5",
      "T": 20.0,
      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.56,
      "dln(kf)_H2O": -2.22,
      "ln(ku)_H2O": 1.95,
      "dln(ku)_H2O": -0.7,
      "dGKIN_H2O": 8.79,
      "ddGKIN_H2O": -3.71,
      "mf": -2.51,
      "mu": 1.09,
      "PhiF_H2O": 1.43,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "L653A",
      "MUTATION_PDB": "L68A",
      "SEC_STR": "Helix",
      "RSA": "5.5",
      "T": 20.0,
      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.56,
      "dln(kf)_H2O": -2.22,
      "ln(ku)_H2O": 1.95,
      "dln(ku)_H2O": -0.7,
      "dGKIN_H2O": 8.79,
      "ddGKIN_H2O": -3.71,
      "mf": -2.51,
      "mu": 1.09,
      "PhiF_H2O": 1.43,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
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         "1sb0A00 (1.10.246.20)"
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Mus musculus",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "PF02172"
      ],
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         "1sb0A00 (1.10.246.20)"
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      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dln(ku)_H2O": -1.1,
      "dGKIN_H2O": 12.59,
      "ddGKIN_H2O": 0.09,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
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         "PF02172"
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         "1sb0A00 (1.10.246.20)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "MUTATION_UNIPROT": "L628,Y658A",
      "MUTATION_PDB": "L43A,Y73A",
      "SEC_STR": "Helix,Helix",
      "RSA": "17.7,57.7",
      "T": 20.0,
      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.89,
      "dln(kf)_H2O": -0.89,
      "ln(ku)_H2O": 0.1,
      "dln(ku)_H2O": -2.55,
      "dGKIN_H2O": 16.54,
      "ddGKIN_H2O": 4.04,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "L628,Y658A",
      "MUTATION_PDB": "L43A,Y73A",
      "SEC_STR": "Helix,Helix",
      "RSA": "17.7,57.7",
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      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.89,
      "dln(kf)_H2O": -0.89,
      "ln(ku)_H2O": 0.1,
      "dln(ku)_H2O": -2.55,
      "dGKIN_H2O": 16.54,
      "ddGKIN_H2O": 4.04,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "Y650,Y658A",
      "MUTATION_PDB": "Y65A,Y73A",
      "SEC_STR": "Helix,Helix",
      "RSA": "41.0,57.7",
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      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.55,
      "dln(kf)_H2O": -0.23,
      "ln(ku)_H2O": 3.43,
      "dln(ku)_H2O": 0.78,
      "dGKIN_H2O": 10.04,
      "ddGKIN_H2O": -2.46,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "Y650,Y658A",
      "MUTATION_PDB": "Y65A,Y73A",
      "SEC_STR": "Helix,Helix",
      "RSA": "41.0,57.7",
      "T": 20.0,
      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.55,
      "dln(kf)_H2O": -0.23,
      "ln(ku)_H2O": 3.43,
      "dln(ku)_H2O": 0.78,
      "dGKIN_H2O": 10.04,
      "ddGKIN_H2O": -2.46,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "L652,Y658A",
      "MUTATION_PDB": "L67A,Y73A",
      "SEC_STR": "Helix,Helix",
      "RSA": "23.2,57.7",
      "T": 20.0,
      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.44,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": 3.26,
      "dln(ku)_H2O": 0.61,
      "dGKIN_H2O": 10.18,
      "ddGKIN_H2O": -2.32,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
      ],
      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "L652,Y658A",
      "MUTATION_PDB": "L67A,Y73A",
      "SEC_STR": "Helix,Helix",
      "RSA": "23.2,57.7",
      "T": 20.0,
      "pH": 7.2,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.44,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": 3.26,
      "dln(ku)_H2O": 0.61,
      "dGKIN_H2O": 10.18,
      "ddGKIN_H2O": -2.32,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I860A",
      "MUTATION_PDB": "I860A",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.37,
      "dln(kf)_H2O": -2.06,
      "ln(ku)_H2O": -8.2,
      "dln(ku)_H2O": 1.42,
      "PhiF_H2O": 0.6,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I860A",
      "MUTATION_PDB": "I860A",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.37,
      "dln(kf)_H2O": -2.06,
      "ln(ku)_H2O": -8.2,
      "dln(ku)_H2O": 1.42,
      "PhiF_H2O": 0.6,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L863A",
      "MUTATION_PDB": "L863A",
      "SEC_STR": "Coil",
      "RSA": "7.3",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.65,
      "dln(kf)_H2O": -2.34,
      "ln(ku)_H2O": -4.84,
      "dln(ku)_H2O": 4.78,
      "PhiF_H2O": 0.33,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3529",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L863A",
      "MUTATION_PDB": "L863A",
      "SEC_STR": "Coil",
      "RSA": "7.3",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.65,
      "dln(kf)_H2O": -2.34,
      "ln(ku)_H2O": -4.84,
      "dln(ku)_H2O": 4.78,
      "PhiF_H2O": 0.33,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3529",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P865A",
      "MUTATION_PDB": "P865A",
      "SEC_STR": "Coil",
      "RSA": "44.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.95,
      "dln(kf)_H2O": -0.74,
      "ln(ku)_H2O": -8.79,
      "dln(ku)_H2O": 0.83,
      "PhiF_H2O": 0.47,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P865A",
      "MUTATION_PDB": "P865A",
      "SEC_STR": "Coil",
      "RSA": "44.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.95,
      "dln(kf)_H2O": -0.74,
      "ln(ku)_H2O": -8.79,
      "dln(ku)_H2O": 0.83,
      "PhiF_H2O": 0.47,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T867S",
      "MUTATION_PDB": "T867S",
      "SEC_STR": "Coil",
      "RSA": "12.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.46,
      "dln(kf)_H2O": -1.23,
      "ln(ku)_H2O": -8.8,
      "dln(ku)_H2O": 0.82,
      "PhiF_H2O": 0.6,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3530",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T867S",
      "MUTATION_PDB": "T867S",
      "SEC_STR": "Coil",
      "RSA": "12.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.46,
      "dln(kf)_H2O": -1.23,
      "ln(ku)_H2O": -8.8,
      "dln(ku)_H2O": 0.82,
      "PhiF_H2O": 0.6,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3530",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T867A",
      "MUTATION_PDB": "T867A",
      "SEC_STR": "Coil",
      "RSA": "12.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.88,
      "dln(kf)_H2O": -0.81,
      "ln(ku)_H2O": -7.12,
      "dln(ku)_H2O": 2.5,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T867A",
      "MUTATION_PDB": "T867A",
      "SEC_STR": "Coil",
      "RSA": "12.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.88,
      "dln(kf)_H2O": -0.81,
      "ln(ku)_H2O": -7.12,
      "dln(ku)_H2O": 2.5,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y869F",
      "MUTATION_PDB": "Y869F",
      "SEC_STR": "Beta",
      "RSA": "4.1",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.53,
      "dln(kf)_H2O": -2.22,
      "ln(ku)_H2O": -6.56,
      "dln(ku)_H2O": 3.06,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3531",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y869F",
      "MUTATION_PDB": "Y869F",
      "SEC_STR": "Beta",
      "RSA": "4.1",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.53,
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      "ln(ku)_H2O": -6.56,
      "dln(ku)_H2O": 3.06,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3531",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "V871A",
      "MUTATION_PDB": "V871A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.87,
      "dln(kf)_H2O": -2.56,
      "ln(ku)_H2O": -7.44,
      "dln(ku)_H2O": 2.18,
      "PhiF_H2O": 0.54,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "V871A",
      "MUTATION_PDB": "V871A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.87,
      "dln(kf)_H2O": -2.56,
      "ln(ku)_H2O": -7.44,
      "dln(ku)_H2O": 2.18,
      "PhiF_H2O": 0.54,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L873A",
      "MUTATION_PDB": "L873A",
      "SEC_STR": "Beta",
      "RSA": "0.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.22,
      "dln(kf)_H2O": -1.47,
      "ln(ku)_H2O": -5.93,
      "dln(ku)_H2O": 3.69,
      "PhiF_H2O": 0.29,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3532",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L873A",
      "MUTATION_PDB": "L873A",
      "SEC_STR": "Beta",
      "RSA": "0.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.22,
      "dln(kf)_H2O": -1.47,
      "ln(ku)_H2O": -5.93,
      "dln(ku)_H2O": 3.69,
      "PhiF_H2O": 0.29,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3532",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "S875A",
      "MUTATION_PDB": "S875A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.47,
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      "ln(ku)_H2O": -9.91,
      "dln(ku)_H2O": -0.29,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "S875A",
      "MUTATION_PDB": "S875A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.47,
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      "ln(ku)_H2O": -9.91,
      "dln(ku)_H2O": -0.29,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "G878A",
      "MUTATION_PDB": "G878A",
      "SEC_STR": "Coil",
      "RSA": "42.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.33,
      "dln(kf)_H2O": -0.36,
      "ln(ku)_H2O": -8.28,
      "dln(ku)_H2O": 1.34,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3533",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "G878A",
      "MUTATION_PDB": "G878A",
      "SEC_STR": "Coil",
      "RSA": "42.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.33,
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      "ln(ku)_H2O": -8.28,
      "dln(ku)_H2O": 1.34,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3533",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "S882A",
      "MUTATION_PDB": "S882A",
      "SEC_STR": "Coil",
      "RSA": "6.2",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.55,
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      "ln(ku)_H2O": -5.0,
      "dln(ku)_H2O": 4.62,
      "PhiF_H2O": 0.03,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "S882A",
      "MUTATION_PDB": "S882A",
      "SEC_STR": "Coil",
      "RSA": "6.2",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.55,
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      "ln(ku)_H2O": -5.0,
      "dln(ku)_H2O": 4.62,
      "PhiF_H2O": 0.03,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P884A",
      "MUTATION_PDB": "P884A",
      "SEC_STR": "Coil",
      "RSA": "51.5",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.6,
      "dln(kf)_H2O": -0.09,
      "ln(ku)_H2O": -9.53,
      "dln(ku)_H2O": 0.09,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3534",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P884A",
      "MUTATION_PDB": "P884A",
      "SEC_STR": "Coil",
      "RSA": "51.5",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.6,
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      "ln(ku)_H2O": -9.53,
      "dln(ku)_H2O": 0.09,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3534",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "A885G",
      "MUTATION_PDB": "A885G",
      "SEC_STR": "Beta",
      "RSA": "26.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.3,
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      "ln(ku)_H2O": -8.17,
      "dln(ku)_H2O": 1.45,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "A885G",
      "MUTATION_PDB": "A885G",
      "SEC_STR": "Beta",
      "RSA": "26.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.3,
      "dln(kf)_H2O": -0.39,
      "ln(ku)_H2O": -8.17,
      "dln(ku)_H2O": 1.45,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "E887A",
      "MUTATION_PDB": "E887A",
      "SEC_STR": "Beta",
      "RSA": "36.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.9,
      "dln(kf)_H2O": 0.21,
      "ln(ku)_H2O": -12.13,
      "dln(ku)_H2O": -2.51,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3535",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "E887A",
      "MUTATION_PDB": "E887A",
      "SEC_STR": "Beta",
      "RSA": "36.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.9,
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      "ln(ku)_H2O": -12.13,
      "dln(ku)_H2O": -2.51,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3535",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "E887G",
      "MUTATION_PDB": "E887G",
      "SEC_STR": "Beta",
      "RSA": "36.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "dln(kf)_H2O": -0.05,
      "ln(ku)_H2O": -9.1,
      "dln(ku)_H2O": 0.52,
      "PhiF_H2O": 0.09,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "E887G",
      "MUTATION_PDB": "E887G",
      "SEC_STR": "Beta",
      "RSA": "36.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.64,
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      "ln(ku)_H2O": -9.1,
      "dln(ku)_H2O": 0.52,
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "F889A",
      "MUTATION_PDB": "F889A",
      "SEC_STR": "Beta",
      "RSA": "8.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.7,
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      "ln(ku)_H2O": -1.44,
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      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3536",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "F889A",
      "MUTATION_PDB": "F889A",
      "SEC_STR": "Beta",
      "RSA": "8.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.7,
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      "ln(ku)_H2O": -1.44,
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      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3536",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T891S",
      "MUTATION_PDB": "T891S",
      "SEC_STR": "Coil",
      "RSA": "17.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T891S",
      "MUTATION_PDB": "T891S",
      "SEC_STR": "Coil",
      "RSA": "17.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T891A",
      "MUTATION_PDB": "T891A",
      "SEC_STR": "Coil",
      "RSA": "17.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.09,
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      "ln(ku)_H2O": -4.43,
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      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3537",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "T891A",
      "MUTATION_PDB": "T891A",
      "SEC_STR": "Coil",
      "RSA": "17.6",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "ln(ku)_H2O": -4.43,
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3537",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L893A",
      "MUTATION_PDB": "L893A",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.7,
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      "ln(ku)_H2O": -9.53,
      "dln(ku)_H2O": 0.09,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L893A",
      "MUTATION_PDB": "L893A",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.7,
      "dln(kf)_H2O": 0.01,
      "ln(ku)_H2O": -9.53,
      "dln(ku)_H2O": 0.09,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I860A,V871A",
      "MUTATION_PDB": "I860A,V871A",
      "SEC_STR": "Beta,Beta",
      "RSA": "1.8,0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -2.3,
      "dln(kf)_H2O": -3.99,
      "ln(ku)_H2O": -5.74,
      "dln(ku)_H2O": 3.88,
      "PhiF_H2O": 0.51,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3538",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I860A,V871A",
      "MUTATION_PDB": "I860A,V871A",
      "SEC_STR": "Beta,Beta",
      "RSA": "1.8,0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -2.3,
      "dln(kf)_H2O": -3.99,
      "ln(ku)_H2O": -5.74,
      "dln(ku)_H2O": 3.88,
      "PhiF_H2O": 0.51,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3538",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.69,
      "ln(ku)_H2O": -9.62,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3517",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
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      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.69,
      "ln(ku)_H2O": -9.62,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3517",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L803A",
      "MUTATION_PDB": "L803A",
      "SEC_STR": "Coil",
      "RSA": "37.2",
      "T": 25.0,
      "pH": 5.0,
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.55,
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      "ln(ku)_H2O": -6.2,
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      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3517",
      "YEAR_KIN": 2000.0,
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      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L803A",
      "MUTATION_PDB": "L803A",
      "SEC_STR": "Coil",
      "RSA": "37.2",
      "T": 25.0,
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "ln(ku)_H2O": -6.2,
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3517",
      "YEAR_KIN": 2000.0,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
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         "PF00041"
      ],
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         "1tenA00 (2.60.40.10)"
      ],
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      "MUTATION_PDB": "P806A",
      "SEC_STR": "Coil",
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P806A",
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      "SEC_STR": "Coil",
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "YEAR_KIN": 2000.0,
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      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I809V",
      "MUTATION_PDB": "I809V",
      "SEC_STR": "Beta",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3518",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1tenA00 (2.60.40.10)"
      ],
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      "SEC_STR": "Beta",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3518",
      "YEAR_KIN": 2000.0,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
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         "1tenA00 (2.60.40.10)"
      ],
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      "SEC_STR": "Beta",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
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      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
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      "SEC_STR": "Beta",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
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      "MUTATION_PDB": "V811A",
      "SEC_STR": "Beta",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3519",
      "YEAR_KIN": 2000.0,
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      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "V811A",
      "MUTATION_PDB": "V811A",
      "SEC_STR": "Beta",
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      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3519",
      "YEAR_KIN": 2000.0,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
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      "MUTATION_PDB": "A819G",
      "SEC_STR": "Beta",
      "RSA": "2.8",
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      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "A819G",
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      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I821V",
      "MUTATION_PDB": "I821V",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "ln(ku)_H2O": -9.86,
      "dln(ku)_H2O": -0.24,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3520",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I821V",
      "MUTATION_PDB": "I821V",
      "SEC_STR": "Beta",
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
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      "ln(ku)_H2O": -9.86,
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      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3520",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I821A",
      "MUTATION_PDB": "I821A",
      "SEC_STR": "Beta",
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      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.71,
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      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I821A",
      "MUTATION_PDB": "I821A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.71,
      "dln(kf)_H2O": -2.4,
      "ln(ku)_H2O": -5.82,
      "dln(ku)_H2O": 3.8,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P826A",
      "MUTATION_PDB": "P826A",
      "SEC_STR": "Coil",
      "RSA": "2.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 2.13,
      "dln(kf)_H2O": 0.44,
      "ln(ku)_H2O": -6.26,
      "dln(ku)_H2O": 3.36,
      "PhiF_H2O": -0.1,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3521",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P826A",
      "MUTATION_PDB": "P826A",
      "SEC_STR": "Coil",
      "RSA": "2.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 2.13,
      "dln(kf)_H2O": 0.44,
      "ln(ku)_H2O": -6.26,
      "dln(ku)_H2O": 3.36,
      "PhiF_H2O": -0.1,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3521",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I830V",
      "MUTATION_PDB": "I830V",
      "SEC_STR": "Coil",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.54,
      "dln(kf)_H2O": -0.15,
      "ln(ku)_H2O": -9.23,
      "dln(ku)_H2O": 0.39,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I830V",
      "MUTATION_PDB": "I830V",
      "SEC_STR": "Coil",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.54,
      "dln(kf)_H2O": -0.15,
      "ln(ku)_H2O": -9.23,
      "dln(ku)_H2O": 0.39,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I830A",
      "MUTATION_PDB": "I830A",
      "SEC_STR": "Coil",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.39,
      "dln(kf)_H2O": -0.3,
      "ln(ku)_H2O": -7.59,
      "dln(ku)_H2O": 2.03,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3522",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I830A",
      "MUTATION_PDB": "I830A",
      "SEC_STR": "Coil",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.39,
      "dln(kf)_H2O": -0.3,
      "ln(ku)_H2O": -7.59,
      "dln(ku)_H2O": 2.03,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3522",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I833V",
      "MUTATION_PDB": "I833V",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.31,
      "dln(kf)_H2O": -0.38,
      "ln(ku)_H2O": -9.16,
      "dln(ku)_H2O": 0.46,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I833V",
      "MUTATION_PDB": "I833V",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.31,
      "dln(kf)_H2O": -0.38,
      "ln(ku)_H2O": -9.16,
      "dln(ku)_H2O": 0.46,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I833A",
      "MUTATION_PDB": "I833A",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.66,
      "dln(kf)_H2O": -1.03,
      "ln(ku)_H2O": -5.12,
      "dln(ku)_H2O": 4.5,
      "PhiF_H2O": 0.19,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3523",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I833A",
      "MUTATION_PDB": "I833A",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.66,
      "dln(kf)_H2O": -1.03,
      "ln(ku)_H2O": -5.12,
      "dln(ku)_H2O": 4.5,
      "PhiF_H2O": 0.19,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3523",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L835A",
      "MUTATION_PDB": "L835A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.82,
      "dln(kf)_H2O": -2.51,
      "ln(ku)_H2O": -4.89,
      "dln(ku)_H2O": 4.73,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L835A",
      "MUTATION_PDB": "L835A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.82,
      "dln(kf)_H2O": -2.51,
      "ln(ku)_H2O": -4.89,
      "dln(ku)_H2O": 4.73,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y837F",
      "MUTATION_PDB": "Y837F",
      "SEC_STR": "Beta",
      "RSA": "17.1",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.74,
      "dln(kf)_H2O": 0.05,
      "ln(ku)_H2O": -8.83,
      "dln(ku)_H2O": 0.79,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3524",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y837F",
      "MUTATION_PDB": "Y837F",
      "SEC_STR": "Beta",
      "RSA": "17.1",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.74,
      "dln(kf)_H2O": 0.05,
      "ln(ku)_H2O": -8.83,
      "dln(ku)_H2O": 0.79,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3524",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y837A",
      "MUTATION_PDB": "Y837A",
      "SEC_STR": "Beta",
      "RSA": "17.1",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -2.04,
      "dln(kf)_H2O": -3.73,
      "ln(ku)_H2O": -6.23,
      "dln(ku)_H2O": 3.39,
      "PhiF_H2O": 0.53,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y837A",
      "MUTATION_PDB": "Y837A",
      "SEC_STR": "Beta",
      "RSA": "17.1",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -2.04,
      "dln(kf)_H2O": -3.73,
      "ln(ku)_H2O": -6.23,
      "dln(ku)_H2O": 3.39,
      "PhiF_H2O": 0.53,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P843A",
      "MUTATION_PDB": "P843A",
      "SEC_STR": "Coil",
      "RSA": "82.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.81,
      "dln(kf)_H2O": -0.88,
      "ln(ku)_H2O": -9.73,
      "dln(ku)_H2O": -0.11,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3525",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "P843A",
      "MUTATION_PDB": "P843A",
      "SEC_STR": "Coil",
      "RSA": "82.4",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.81,
      "dln(kf)_H2O": -0.88,
      "ln(ku)_H2O": -9.73,
      "dln(ku)_H2O": -0.11,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3525",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "G844A",
      "MUTATION_PDB": "G844A",
      "SEC_STR": "Coil",
      "RSA": "90.5",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.6,
      "dln(kf)_H2O": -0.09,
      "ln(ku)_H2O": -9.12,
      "dln(ku)_H2O": 0.5,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "G844A",
      "MUTATION_PDB": "G844A",
      "SEC_STR": "Coil",
      "RSA": "90.5",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 1.6,
      "dln(kf)_H2O": -0.09,
      "ln(ku)_H2O": -9.12,
      "dln(ku)_H2O": 0.5,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I849A",
      "MUTATION_PDB": "I849A",
      "SEC_STR": "Beta",
      "RSA": "21.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.76,
      "dln(kf)_H2O": -2.45,
      "ln(ku)_H2O": -8.38,
      "dln(ku)_H2O": 1.24,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3526",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I849A",
      "MUTATION_PDB": "I849A",
      "SEC_STR": "Beta",
      "RSA": "21.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.76,
      "dln(kf)_H2O": -2.45,
      "ln(ku)_H2O": -8.38,
      "dln(ku)_H2O": 1.24,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3526",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L851A",
      "MUTATION_PDB": "L851A",
      "SEC_STR": "Beta",
      "RSA": "4.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.43,
      "dln(kf)_H2O": -2.12,
      "ln(ku)_H2O": -6.69,
      "dln(ku)_H2O": 2.93,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "L851A",
      "MUTATION_PDB": "L851A",
      "SEC_STR": "Beta",
      "RSA": "4.9",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.43,
      "dln(kf)_H2O": -2.12,
      "ln(ku)_H2O": -6.69,
      "dln(ku)_H2O": 2.93,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y858A",
      "MUTATION_PDB": "Y858A",
      "SEC_STR": "Beta",
      "RSA": "30.2",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.82,
      "dln(kf)_H2O": -0.87,
      "ln(ku)_H2O": -8.16,
      "dln(ku)_H2O": 1.46,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3527",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y858A",
      "MUTATION_PDB": "Y858A",
      "SEC_STR": "Beta",
      "RSA": "30.2",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.82,
      "dln(kf)_H2O": -0.87,
      "ln(ku)_H2O": -8.16,
      "dln(ku)_H2O": 1.46,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3527",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y858G",
      "MUTATION_PDB": "Y858G",
      "SEC_STR": "Beta",
      "RSA": "30.2",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.03,
      "dln(kf)_H2O": -1.72,
      "ln(ku)_H2O": -4.35,
      "dln(ku)_H2O": 5.27,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "Y858G",
      "MUTATION_PDB": "Y858G",
      "SEC_STR": "Beta",
      "RSA": "30.2",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": -0.03,
      "dln(kf)_H2O": -1.72,
      "ln(ku)_H2O": -4.35,
      "dln(ku)_H2O": 5.27,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78.",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I860V",
      "MUTATION_PDB": "I860V",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.8,
      "dln(kf)_H2O": -0.89,
      "ln(ku)_H2O": -9.11,
      "dln(ku)_H2O": 0.51,
      "PhiF_H2O": 0.64,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3528",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Tenascin, TNfn3 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 92.0,
      "UniProt": "P24821",
      "PDB_wild": "1ten",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00041"
      ],
      "CATH": [
         "1tenA00 (2.60.40.10)"
      ],
      "MUTATION_UNIPROT": "I860V",
      "MUTATION_PDB": "I860V",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "alkaline unfolding (pH 12.4)",
      "ln(kf)_H2O": 0.8,
      "dln(kf)_H2O": -0.89,
      "ln(ku)_H2O": -9.11,
      "dln(ku)_H2O": 0.51,
      "PhiF_H2O": 0.64,
      "AUTHOR_KIN": "Hamill SJ, Steward A, Clarke J",
      "REFERENCE_KIN": "The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J Mol Biol. 297(1):165-78. https://doi.org/10.1006/jmbi.2000.3528",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10704314",
      "STATE": "Yes",
      "REVERSIBILITY": "Yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Nucleophosmin, Cter-NPM1 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 10.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.0,
      "ln(ku)_H2O": 1.06,
      "dGKIN_H2O": 13.97,
      "mf": -3.14,
      "mu": 1.13,
      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Nucleophosmin, Cter-NPM1 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 10.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.0,
      "ln(ku)_H2O": 1.06,
      "dGKIN_H2O": 13.97,
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "V244A",
      "MUTATION_PDB": "V4A",
      "SEC_STR": "Helix",
      "RSA": "28.2",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
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      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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      ],
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "MUTATION_PDB": "E5A",
      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "A245G",
      "MUTATION_PDB": "A5G",
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      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "MUTATION_PDB": "A5G",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "D246A",
      "MUTATION_PDB": "D6A",
      "SEC_STR": "Helix",
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      "BUFFER_NAME": "Sodium Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "D246A",
      "MUTATION_PDB": "D6A",
      "SEC_STR": "Helix",
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      "BUFFER_NAME": "Sodium Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "A246G",
      "MUTATION_PDB": "A6G",
      "T": 10.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Nucleophosmin, Cter-NPM1 domain",
      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
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      "MUTATION_UNIPROT": "A246G",
      "MUTATION_PDB": "A6G",
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      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
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         "PF16276"
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "I247V",
      "MUTATION_PDB": "I7V",
      "SEC_STR": "Helix",
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      "BUFFER_NAME": "Sodium Phosphate",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
      "MUTATION_UNIPROT": "A249G",
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      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
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         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
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      "MUTATION_PDB": "A9G",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "MUTATION_PDB": "A10G",
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      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
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      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
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      "SEC_STR": "Coil",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
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      "CATH": [
         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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   },
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dln(ku)_H2O": -0.03,
      "dGKIN_H2O": 12.99,
      "ddGKIN_H2O": -0.96,
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      "mu": 1.09,
      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 52.0,
      "UniProt": "P06748",
      "PDB_wild": "2vxd",
      "MUTATED_CHAIN": "A",
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         "PF16276"
      ],
      "CATH": [
         "2vxdA00 (1.10.10.2100)"
      ],
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      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06748",
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         "PF16276"
      ],
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         "2vxdA00 (1.10.10.2100)"
      ],
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      ],
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06748",
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "SOURCE": "Homo sapiens",
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "SOURCE": "Homo sapiens",
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         "PF16276"
      ],
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "BUFFER_CONC": "0.05",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
      "YEAR_KIN": 2010.0,
      "PMID_KIN": "20212148",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
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      ],
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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         "2vxdA00 (1.10.10.2100)"
      ],
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "2vxdA00 (1.10.10.2100)"
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         "2vxdA00 (1.10.10.2100)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06748",
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06748",
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         "2vxdA00 (1.10.10.2100)"
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      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06748",
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      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S",
      "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107",
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      "PMID_KIN": "20212148",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
      "UniProt": "O75400",
      "PDB_wild": "1uzc",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01846"
      ],
      "CATH": [
         "1uzcA00 (1.10.10.440)"
      ],
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      "AUTHOR_KIN": "Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR",
      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15935381",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
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      "MUTATED_CHAIN": "A",
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         "PF01846"
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         "1uzcA00 (1.10.10.440)"
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      "MUTATION_PDB": "WT",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
      "UniProt": "O75400",
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         "1uzcA00 (1.10.10.440)"
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      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FF domain from HYPA/FBP11",
      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
      "UniProt": "O75400",
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "PROTEIN": "FF domain from HYPA/FBP11",
      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
      "UniProt": "O75400",
      "PDB_wild": "1uzc",
      "MUTATED_CHAIN": "A",
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      ],
      "CATH": [
         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
      "UniProt": "O75400",
      "PDB_wild": "1uzc",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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         "PF01846"
      ],
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         "1uzcA00 (1.10.10.440)"
      ],
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      "AUTHOR_KIN": "Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR",
      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
      "YEAR_KIN": 2005.0,
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      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
      ],
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         "1uzcA00 (1.10.10.440)"
      ],
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
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      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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      "MUTATED_CHAIN": "A",
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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      "PDB_wild": "1uzc",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01846"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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      ],
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         "1uzcA00 (1.10.10.440)"
      ],
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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      "SOURCE": "Homo sapiens",
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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         "1uzcA00 (1.10.10.440)"
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      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FF domain from HYPA/FBP11",
      "SOURCE": "Homo sapiens",
      "LENGTH": 70.0,
      "UniProt": "O75400",
      "PDB_wild": "1uzc",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01846"
      ],
      "CATH": [
         "1uzcA00 (1.10.10.440)"
      ],
      "MUTATION_UNIPROT": "V446G",
      "MUTATION_PDB": "V67G",
      "SEC_STR": "Helix",
      "RSA": "70.4",
      "T": 10.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na-Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.77,
      "dln(kf)_H2O": 0.07,
      "ln(ku)_H2O": 1.46,
      "dln(ku)_H2O": 0.16,
      "dGKIN_H2O": 15.06,
      "ddGKIN_H2O": -0.17,
      "mf": -4.09,
      "mu": -0.57,
      "AUTHOR_KIN": "Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR",
      "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15935381",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.77,
      "ln(ku)_H2O": -1.97,
      "dGKIN_H2O": 11.74,
      "mf": -2.47,
      "mu": 0.59,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.77,
      "ln(ku)_H2O": -1.97,
      "dGKIN_H2O": 11.74,
      "mf": -2.47,
      "mu": 0.59,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "T159S",
      "MUTATION_PDB": "T1S",
      "SEC_STR": "Coil",
      "RSA": "82.4",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.56,
      "dln(kf)_H2O": -0.21,
      "ln(ku)_H2O": -1.56,
      "dln(ku)_H2O": 0.41,
      "dGKIN_H2O": 10.21,
      "ddGKIN_H2O": -1.53,
      "mf": -2.47,
      "mu": 0.5,
      "PhiF_H2O": 0.28,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "T159S",
      "MUTATION_PDB": "T1S",
      "SEC_STR": "Coil",
      "RSA": "82.4",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.56,
      "dln(kf)_H2O": -0.21,
      "ln(ku)_H2O": -1.56,
      "dln(ku)_H2O": 0.41,
      "dGKIN_H2O": 10.21,
      "ddGKIN_H2O": -1.53,
      "mf": -2.47,
      "mu": 0.5,
      "PhiF_H2O": 0.28,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "Y160A",
      "MUTATION_PDB": "Y2A",
      "SEC_STR": "Beta",
      "RSA": "51.8",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.15,
      "dln(kf)_H2O": -0.62,
      "ln(ku)_H2O": -0.37,
      "dln(ku)_H2O": 1.6,
      "dGKIN_H2O": 6.24,
      "ddGKIN_H2O": -5.5,
      "mf": -2.47,
      "mu": 0.29,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "Y160A",
      "MUTATION_PDB": "Y2A",
      "SEC_STR": "Beta",
      "RSA": "51.8",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.15,
      "dln(kf)_H2O": -0.62,
      "ln(ku)_H2O": -0.37,
      "dln(ku)_H2O": 1.6,
      "dGKIN_H2O": 6.24,
      "ddGKIN_H2O": -5.5,
      "mf": -2.47,
      "mu": 0.29,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V161A",
      "MUTATION_PDB": "V3A",
      "SEC_STR": "Beta",
      "RSA": "0.7",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.53,
      "dln(kf)_H2O": -1.24,
      "ln(ku)_H2O": -1.11,
      "dln(ku)_H2O": 0.86,
      "dGKIN_H2O": 6.54,
      "ddGKIN_H2O": -5.2,
      "mf": -3.14,
      "mu": 0.33,
      "PhiF_H2O": 0.58,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V161A",
      "MUTATION_PDB": "V3A",
      "SEC_STR": "Beta",
      "RSA": "0.7",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.53,
      "dln(kf)_H2O": -1.24,
      "ln(ku)_H2O": -1.11,
      "dln(ku)_H2O": 0.86,
      "dGKIN_H2O": 6.54,
      "ddGKIN_H2O": -5.2,
      "mf": -3.14,
      "mu": 0.33,
      "PhiF_H2O": 0.58,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A163G",
      "MUTATION_PDB": "A5G",
      "SEC_STR": "Beta",
      "RSA": "4.7",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.53,
      "dln(kf)_H2O": -2.24,
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      "dln(ku)_H2O": 0.95,
      "dGKIN_H2O": 3.84,
      "ddGKIN_H2O": -7.9,
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      "mu": 0.5,
      "PhiF_H2O": 0.7,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A163G",
      "MUTATION_PDB": "A5G",
      "SEC_STR": "Beta",
      "RSA": "4.7",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.53,
      "dln(kf)_H2O": -2.24,
      "ln(ku)_H2O": -1.02,
      "dln(ku)_H2O": 0.95,
      "dGKIN_H2O": 3.84,
      "ddGKIN_H2O": -7.9,
      "mf": -2.64,
      "mu": 0.5,
      "PhiF_H2O": 0.7,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L164A",
      "MUTATION_PDB": "L6A",
      "SEC_STR": "Coil",
      "RSA": "47.0",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.08,
      "dln(kf)_H2O": -0.69,
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      "dln(ku)_H2O": 1.57,
      "dGKIN_H2O": 6.14,
      "ddGKIN_H2O": -5.6,
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      "mu": 0.54,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L164A",
      "MUTATION_PDB": "L6A",
      "SEC_STR": "Coil",
      "RSA": "47.0",
      "T": 22.0,
      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.08,
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      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "2vwfA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "F165A",
      "MUTATION_PDB": "F7A",
      "SEC_STR": "Coil",
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      "pH": 7.2,
      "BUFFER_NAME": "NaPi",
      "BUFFER_CONC": "0.05",
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      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Grb2-SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S",
      "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320",
      "YEAR_KIN": 2018.0,
      "PMID_KIN": "30091591",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
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         "2vwfA00 (2.30.30.40)"
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      "SEC_STR": "Beta",
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      "PMID_KIN": "30091591",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "2vwfA00 (2.30.30.40)"
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      "SEC_STR": "Beta",
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      "PMID_KIN": "30091591",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
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         "2vwfA00 (2.30.30.40)"
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      "BUFFER_CONC": "0.05",
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      "PMID_KIN": "30091591",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
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      "SEC_STR": "Helix",
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      "PMID_KIN": "30091591",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
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      "SEC_STR": "Beta",
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      "PMID_KIN": "30091591",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 56.0,
      "UniProt": "P62993",
      "PDB_wild": "2vwf",
      "MUTATED_CHAIN": "A",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "UniProt": "P62993",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "UniProt": "P62993",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "UniProt": "P62993",
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         "2vwfA00 (2.30.30.40)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "PMID_KIN": "30091591",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Thermus thermophylus",
      "LENGTH": 101.0,
      "UniProt": "P23370",
      "PDB_wild": "1ris",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01250"
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      "CATH": [
         "1risA00 (3.30.70.60)"
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      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 6.3,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 5.83,
      "ln(ku)_H2O": -8.59,
      "dGKIN_H2O": 35.56,
      "mf": -5.06,
      "mu": 2.47,
      "CM_KIN": 3.47,
      "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M",
      "REFERENCE_KIN": "Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17056063",
      "STATE": "Yes",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "UniProt": "P23370",
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      "PFAM": [
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      "CATH": [
         "1risA00 (3.30.70.60)"
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      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
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      "BUFFER_NAME": "MES",
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      "dGKIN_H2O": 35.56,
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      "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "PFAM": [
         "PF01250"
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      "CATH": [
         "2j5aA00 (3.30.70.60)"
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M",
      "REFERENCE_KIN": "Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.52,
      "ln(ku)_H2O": -2.73,
      "dGKIN_H2O": 16.99,
      "mf": -1.44,
      "mu": 3.22,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.52,
      "ln(ku)_H2O": -2.73,
      "dGKIN_H2O": 16.99,
      "mf": -1.44,
      "mu": 3.22,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "I6V",
      "MUTATION_PDB": "I6V",
      "SEC_STR": "Coil",
      "RSA": "26.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.17,
      "dln(kf)_H2O": -0.35,
      "ln(ku)_H2O": -1.31,
      "dln(ku)_H2O": 1.42,
      "dGKIN_H2O": 12.84,
      "ddGKIN_H2O": -4.15,
      "mf": -1.34,
      "mu": 2.85,
      "PhiF_H2O": 0.49,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "I6V",
      "MUTATION_PDB": "I6V",
      "SEC_STR": "Coil",
      "RSA": "26.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.17,
      "dln(kf)_H2O": -0.35,
      "ln(ku)_H2O": -1.31,
      "dln(ku)_H2O": 1.42,
      "dGKIN_H2O": 12.84,
      "ddGKIN_H2O": -4.15,
      "mf": -1.34,
      "mu": 2.85,
      "PhiF_H2O": 0.49,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "Y8A",
      "MUTATION_PDB": "Y8A",
      "SEC_STR": "Beta",
      "RSA": "34.7",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.22,
      "dln(kf)_H2O": -0.3,
      "ln(ku)_H2O": -2.17,
      "dln(ku)_H2O": 0.56,
      "dGKIN_H2O": 14.98,
      "ddGKIN_H2O": -2.01,
      "mf": -1.06,
      "mu": 3.13,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "Y8A",
      "MUTATION_PDB": "Y8A",
      "SEC_STR": "Beta",
      "RSA": "34.7",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.22,
      "dln(kf)_H2O": -0.3,
      "ln(ku)_H2O": -2.17,
      "dln(ku)_H2O": 0.56,
      "dGKIN_H2O": 14.98,
      "ddGKIN_H2O": -2.01,
      "mf": -1.06,
      "mu": 3.13,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "S9A",
      "MUTATION_PDB": "S9A",
      "SEC_STR": "Coil",
      "RSA": "23.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.25,
      "dln(kf)_H2O": -0.27,
      "ln(ku)_H2O": -2.62,
      "dln(ku)_H2O": 0.11,
      "dGKIN_H2O": 16.11,
      "ddGKIN_H2O": -0.88,
      "mf": -1.11,
      "mu": 3.22,
      "PhiF_H2O": 0.45,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "S9A",
      "MUTATION_PDB": "S9A",
      "SEC_STR": "Coil",
      "RSA": "23.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.25,
      "dln(kf)_H2O": -0.27,
      "ln(ku)_H2O": -2.62,
      "dln(ku)_H2O": 0.11,
      "dGKIN_H2O": 16.11,
      "ddGKIN_H2O": -0.88,
      "mf": -1.11,
      "mu": 3.22,
      "PhiF_H2O": 0.45,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "K11A",
      "MUTATION_PDB": "K11A",
      "SEC_STR": "Coil",
      "RSA": "48.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.31,
      "dln(kf)_H2O": -0.21,
      "ln(ku)_H2O": -3.24,
      "dln(ku)_H2O": -0.51,
      "dGKIN_H2O": 17.7,
      "ddGKIN_H2O": 0.71,
      "mf": -1.11,
      "mu": 3.29,
      "PhiF_H2O": -0.23,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "K11A",
      "MUTATION_PDB": "K11A",
      "SEC_STR": "Coil",
      "RSA": "48.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.31,
      "dln(kf)_H2O": -0.21,
      "ln(ku)_H2O": -3.24,
      "dln(ku)_H2O": -0.51,
      "dGKIN_H2O": 17.7,
      "ddGKIN_H2O": 0.71,
      "mf": -1.11,
      "mu": 3.29,
      "PhiF_H2O": -0.23,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "F17L",
      "MUTATION_PDB": "F17L",
      "SEC_STR": "Beta",
      "RSA": "26.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.13,
      "dln(kf)_H2O": -2.39,
      "ln(ku)_H2O": 1.24,
      "dln(ku)_H2O": 3.97,
      "dGKIN_H2O": 2.09,
      "ddGKIN_H2O": -14.9,
      "mu": 2.28,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "F17L",
      "MUTATION_PDB": "F17L",
      "SEC_STR": "Beta",
      "RSA": "26.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.13,
      "dln(kf)_H2O": -2.39,
      "ln(ku)_H2O": 1.24,
      "dln(ku)_H2O": 3.97,
      "dGKIN_H2O": 2.09,
      "ddGKIN_H2O": -14.9,
      "mu": 2.28,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "E18A",
      "MUTATION_PDB": "E18A",
      "SEC_STR": "Beta",
      "RSA": "14.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.07,
      "dln(kf)_H2O": -2.45,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.2,
      "dGKIN_H2O": 10.75,
      "ddGKIN_H2O": -6.24,
      "mf": -1.65,
      "mu": 3.11,
      "PhiF_H2O": 1.1,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "E18A",
      "MUTATION_PDB": "E18A",
      "SEC_STR": "Beta",
      "RSA": "14.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.07,
      "dln(kf)_H2O": -2.45,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.2,
      "dGKIN_H2O": 10.75,
      "ddGKIN_H2O": -6.24,
      "mf": -1.65,
      "mu": 3.11,
      "PhiF_H2O": 1.1,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V22A",
      "MUTATION_PDB": "V22A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.66,
      "dln(kf)_H2O": -0.86,
      "ln(ku)_H2O": -0.48,
      "dln(ku)_H2O": 2.25,
      "dGKIN_H2O": 9.71,
      "ddGKIN_H2O": -7.28,
      "mf": -1.62,
      "mu": 2.64,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V22A",
      "MUTATION_PDB": "V22A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.66,
      "dln(kf)_H2O": -0.86,
      "ln(ku)_H2O": -0.48,
      "dln(ku)_H2O": 2.25,
      "dGKIN_H2O": 9.71,
      "ddGKIN_H2O": -7.28,
      "mf": -1.62,
      "mu": 2.64,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "L24A",
      "MUTATION_PDB": "L24A",
      "SEC_STR": "Coil",
      "RSA": "0.6",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.59,
      "dln(kf)_H2O": -0.93,
      "ln(ku)_H2O": 2.2,
      "dln(ku)_H2O": 4.93,
      "dGKIN_H2O": 3.26,
      "ddGKIN_H2O": -13.73,
      "mu": 2.16,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "L24A",
      "MUTATION_PDB": "L24A",
      "SEC_STR": "Coil",
      "RSA": "0.6",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.59,
      "dln(kf)_H2O": -0.93,
      "ln(ku)_H2O": 2.2,
      "dln(ku)_H2O": 4.93,
      "dGKIN_H2O": 3.26,
      "ddGKIN_H2O": -13.73,
      "mu": 2.16,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V32A",
      "MUTATION_PDB": "V32A",
      "SEC_STR": "Coil",
      "RSA": "2.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.21,
      "dln(kf)_H2O": -0.31,
      "ln(ku)_H2O": -0.53,
      "dln(ku)_H2O": 2.2,
      "dGKIN_H2O": 11.09,
      "ddGKIN_H2O": -5.9,
      "mf": -1.15,
      "mu": 2.75,
      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V32A",
      "MUTATION_PDB": "V32A",
      "SEC_STR": "Coil",
      "RSA": "2.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.21,
      "dln(kf)_H2O": -0.31,
      "ln(ku)_H2O": -0.53,
      "dln(ku)_H2O": 2.2,
      "dGKIN_H2O": 11.09,
      "ddGKIN_H2O": -5.9,
      "mf": -1.15,
      "mu": 2.75,
      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "S39A",
      "MUTATION_PDB": "S39A",
      "SEC_STR": "Coil",
      "RSA": "45.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.12,
      "dln(kf)_H2O": -0.4,
      "ln(ku)_H2O": -0.54,
      "dln(ku)_H2O": 2.19,
      "dGKIN_H2O": 10.92,
      "ddGKIN_H2O": -6.07,
      "mf": -1.29,
      "mu": 2.71,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "S39A",
      "MUTATION_PDB": "S39A",
      "SEC_STR": "Coil",
      "RSA": "45.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.12,
      "dln(kf)_H2O": -0.4,
      "ln(ku)_H2O": -0.54,
      "dln(ku)_H2O": 2.19,
      "dGKIN_H2O": 10.92,
      "ddGKIN_H2O": -6.07,
      "mf": -1.29,
      "mu": 2.71,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "L46A",
      "MUTATION_PDB": "L46A",
      "SEC_STR": "Helix",
      "RSA": "22.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.09,
      "dln(kf)_H2O": -0.43,
      "ln(ku)_H2O": 0.63,
      "dln(ku)_H2O": 3.36,
      "dGKIN_H2O": 8.12,
      "ddGKIN_H2O": -8.87,
      "mf": -0.99,
      "mu": 2.56,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "L46A",
      "MUTATION_PDB": "L46A",
      "SEC_STR": "Helix",
      "RSA": "22.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.09,
      "dln(kf)_H2O": -0.43,
      "ln(ku)_H2O": 0.63,
      "dln(ku)_H2O": 3.36,
      "dGKIN_H2O": 8.12,
      "ddGKIN_H2O": -8.87,
      "mf": -0.99,
      "mu": 2.56,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V55A",
      "MUTATION_PDB": "V55A",
      "SEC_STR": "Beta",
      "RSA": "59.2",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.28,
      "dln(kf)_H2O": -0.24,
      "ln(ku)_H2O": -0.05,
      "dln(ku)_H2O": 2.68,
      "dGKIN_H2O": 10.13,
      "ddGKIN_H2O": -6.86,
      "mf": -1.53,
      "mu": 2.64,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V55A",
      "MUTATION_PDB": "V55A",
      "SEC_STR": "Beta",
      "RSA": "59.2",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.28,
      "dln(kf)_H2O": -0.24,
      "ln(ku)_H2O": -0.05,
      "dln(ku)_H2O": 2.68,
      "dGKIN_H2O": 10.13,
      "ddGKIN_H2O": -6.86,
      "mf": -1.53,
      "mu": 2.64,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V55G",
      "MUTATION_PDB": "V55G",
      "SEC_STR": "Beta",
      "RSA": "59.2",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.18,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": 1.52,
      "dln(ku)_H2O": 4.25,
      "dGKIN_H2O": 6.23,
      "ddGKIN_H2O": -10.76,
      "mf": -1.46,
      "mu": 2.21,
      "PhiF_H2O": 0.09,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "V55G",
      "MUTATION_PDB": "V55G",
      "SEC_STR": "Beta",
      "RSA": "59.2",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.18,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": 1.52,
      "dln(ku)_H2O": 4.25,
      "dGKIN_H2O": 6.23,
      "ddGKIN_H2O": -10.76,
      "mf": -1.46,
      "mu": 2.21,
      "PhiF_H2O": 0.09,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "M58L",
      "MUTATION_PDB": "M58L",
      "SEC_STR": "Beta",
      "RSA": "53.7",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.15,
      "dln(kf)_H2O": -0.37,
      "ln(ku)_H2O": -1.24,
      "dln(ku)_H2O": 1.49,
      "dGKIN_H2O": 12.64,
      "ddGKIN_H2O": -4.35,
      "mf": -1.2,
      "mu": 2.85,
      "PhiF_H2O": 0.41,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "M58L",
      "MUTATION_PDB": "M58L",
      "SEC_STR": "Beta",
      "RSA": "53.7",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.15,
      "dln(kf)_H2O": -0.37,
      "ln(ku)_H2O": -1.24,
      "dln(ku)_H2O": 1.49,
      "dGKIN_H2O": 12.64,
      "ddGKIN_H2O": -4.35,
      "mf": -1.2,
      "mu": 2.85,
      "PhiF_H2O": 0.41,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "P62A",
      "MUTATION_PDB": "P62A",
      "SEC_STR": "Coil",
      "RSA": "75.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.4,
      "dln(kf)_H2O": 0.88,
      "ln(ku)_H2O": -3.96,
      "dln(ku)_H2O": -1.23,
      "dGKIN_H2O": 21.92,
      "ddGKIN_H2O": 4.93,
      "mf": -1.39,
      "mu": 3.27,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "P62A",
      "MUTATION_PDB": "P62A",
      "SEC_STR": "Coil",
      "RSA": "75.0",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.4,
      "dln(kf)_H2O": 0.88,
      "ln(ku)_H2O": -3.96,
      "dln(ku)_H2O": -1.23,
      "dGKIN_H2O": 21.92,
      "ddGKIN_H2O": 4.93,
      "mf": -1.39,
      "mu": 3.27,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "P64A",
      "MUTATION_PDB": "P64A",
      "SEC_STR": "Coil",
      "RSA": "32.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.34,
      "dln(kf)_H2O": -0.18,
      "ln(ku)_H2O": -1.14,
      "dln(ku)_H2O": 1.59,
      "dGKIN_H2O": 12.84,
      "ddGKIN_H2O": -4.15,
      "mf": -0.52,
      "mu": 2.85,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "P64A",
      "MUTATION_PDB": "P64A",
      "SEC_STR": "Coil",
      "RSA": "32.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.34,
      "dln(kf)_H2O": -0.18,
      "ln(ku)_H2O": -1.14,
      "dln(ku)_H2O": 1.59,
      "dGKIN_H2O": 12.84,
      "ddGKIN_H2O": -4.15,
      "mf": -0.52,
      "mu": 2.85,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "H65A",
      "MUTATION_PDB": "H65A",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.98,
      "dln(kf)_H2O": -0.54,
      "ln(ku)_H2O": -2.85,
      "dln(ku)_H2O": -0.12,
      "dGKIN_H2O": 15.98,
      "ddGKIN_H2O": -1.01,
      "mf": -1.39,
      "mu": 3.29,
      "PhiF_H2O": 0.51,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "H65A",
      "MUTATION_PDB": "H65A",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.98,
      "dln(kf)_H2O": -0.54,
      "ln(ku)_H2O": -2.85,
      "dln(ku)_H2O": -0.12,
      "dGKIN_H2O": 15.98,
      "ddGKIN_H2O": -1.01,
      "mf": -1.39,
      "mu": 3.29,
      "PhiF_H2O": 0.51,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "L67A",
      "MUTATION_PDB": "L67A",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.81,
      "dln(kf)_H2O": -0.71,
      "ln(ku)_H2O": 0.84,
      "dln(ku)_H2O": 3.57,
      "dGKIN_H2O": 6.95,
      "ddGKIN_H2O": -10.04,
      "mf": -1.2,
      "mu": 2.49,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "L67A",
      "MUTATION_PDB": "L67A",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.81,
      "dln(kf)_H2O": -0.71,
      "ln(ku)_H2O": 0.84,
      "dln(ku)_H2O": 3.57,
      "dGKIN_H2O": 6.95,
      "ddGKIN_H2O": -10.04,
      "mf": -1.2,
      "mu": 2.49,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "F69L",
      "MUTATION_PDB": "F69L",
      "SEC_STR": "Beta",
      "RSA": "0.5",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": -0.32,
      "ln(ku)_H2O": 1.41,
      "dln(ku)_H2O": 4.14,
      "dGKIN_H2O": 6.57,
      "ddGKIN_H2O": -10.42,
      "mf": -1.88,
      "mu": 2.38,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "F69L",
      "MUTATION_PDB": "F69L",
      "SEC_STR": "Beta",
      "RSA": "0.5",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": -0.32,
      "ln(ku)_H2O": 1.41,
      "dln(ku)_H2O": 4.14,
      "dGKIN_H2O": 6.57,
      "ddGKIN_H2O": -10.42,
      "mf": -1.88,
      "mu": 2.38,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "R70A",
      "MUTATION_PDB": "R70A",
      "SEC_STR": "Beta",
      "RSA": "29.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.91,
      "dln(kf)_H2O": -1.61,
      "ln(ku)_H2O": 1.6,
      "dln(ku)_H2O": 4.33,
      "dGKIN_H2O": 3.1,
      "ddGKIN_H2O": -13.89,
      "mf": -2.05,
      "mu": 2.09,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "R70A",
      "MUTATION_PDB": "R70A",
      "SEC_STR": "Beta",
      "RSA": "29.8",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.91,
      "dln(kf)_H2O": -1.61,
      "ln(ku)_H2O": 1.6,
      "dln(ku)_H2O": 4.33,
      "dGKIN_H2O": 3.1,
      "ddGKIN_H2O": -13.89,
      "mf": -2.05,
      "mu": 2.09,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "R71A",
      "MUTATION_PDB": "R71A",
      "SEC_STR": "Beta",
      "RSA": "22.6",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.49,
      "dln(kf)_H2O": -0.03,
      "ln(ku)_H2O": -0.42,
      "dln(ku)_H2O": 2.31,
      "dGKIN_H2O": 11.51,
      "ddGKIN_H2O": -5.48,
      "mf": -1.15,
      "mu": 2.75,
      "PhiF_H2O": 0.03,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CKS1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P61024",
      "PDB_wild": "1dkt",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01111"
      ],
      "CATH": [
         "1dktA00 (3.30.170.10)"
      ],
      "MUTATION_UNIPROT": "R71A",
      "MUTATION_PDB": "R71A",
      "SEC_STR": "Beta",
      "RSA": "22.6",
      "T": 10.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.49,
      "dln(kf)_H2O": -0.03,
      "ln(ku)_H2O": -0.42,
      "dln(ku)_H2O": 2.31,
      "dGKIN_H2O": 11.51,
      "ddGKIN_H2O": -5.48,
      "mf": -1.15,
      "mu": 2.75,
      "PhiF_H2O": 0.03,
      "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS",
      "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "12473461",
      "STATE": "Yes",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "I98K,N102I,G106L",
      "MUTATION_PDB": "I98K,N102I,G106L",
      "SEC_STR": "Helix,Helix,Coil",
      "RSA": "37.3,59.2,100.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "NaAcetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.56,
      "ln(ku)_H2O": -0.25,
      "dGKIN_H2O": 11.92,
      "ddGKIN_H2O": -10.2,
      "mf": -3.51,
      "mu": 3.64,
      "PhiF_H2O": 0.11,
      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "I98K,N102I,G106L",
      "MUTATION_PDB": "I98K,N102I,G106L",
      "SEC_STR": "Helix,Helix,Coil",
      "RSA": "37.3,59.2,100.0",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "NaAcetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.56,
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      "dGKIN_H2O": 11.92,
      "ddGKIN_H2O": -10.2,
      "mf": -3.51,
      "mu": 3.64,
      "PhiF_H2O": 0.11,
      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "V69G",
      "MUTATION_PDB": "V69G",
      "SEC_STR": "Helix",
      "RSA": "11.3",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "NaAcetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.48,
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      "ln(ku)_H2O": 0.74,
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      "dGKIN_H2O": 6.78,
      "ddGKIN_H2O": -15.34,
      "mf": -3.05,
      "mu": 3.18,
      "PhiF_H2O": 0.25,
      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "V69G",
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      "SEC_STR": "Helix",
      "RSA": "11.3",
      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "NaAcetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.48,
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      "ln(ku)_H2O": 0.74,
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      "dGKIN_H2O": 6.78,
      "ddGKIN_H2O": -15.34,
      "mf": -3.05,
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      "PhiF_H2O": 0.25,
      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "I72A",
      "MUTATION_PDB": "I72A",
      "SEC_STR": "Helix",
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      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "NaAcetate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "urea",
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      "ln(ku)_H2O": 2.37,
      "dln(ku)_H2O": 6.28,
      "dGKIN_H2O": 1.86,
      "ddGKIN_H2O": -20.25,
      "mf": -4.27,
      "mu": 2.97,
      "PhiF_H2O": 0.23,
      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "I72A",
      "MUTATION_PDB": "I72A",
      "SEC_STR": "Helix",
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      "T": 25.0,
      "pH": 5.0,
      "BUFFER_NAME": "NaAcetate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "urea",
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      "dGKIN_H2O": 1.86,
      "ddGKIN_H2O": -20.25,
      "mf": -4.27,
      "mu": 2.97,
      "PhiF_H2O": 0.23,
      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "D73A",
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      "ddGKIN_H2O": -6.61,
      "mf": -3.47,
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      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "D73A",
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      "mf": -3.47,
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         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "L76A",
      "MUTATION_PDB": "L76A",
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      "T": 25.0,
      "pH": 5.0,
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      "BACKGROUND_MUT_UNIPROT": [
         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "L76A",
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         "M7W",
         "R98I",
         "N99R",
         "H102N",
         "R106G"
      ],
      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
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         "M7W",
         "R98I",
         "N99R",
         "H102N",
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      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12069590",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Rd-apocyt b562 (de novo)",
      "SOURCE": "Escherichia coli",
      "LENGTH": 106.0,
      "UniProt": "P0ABE7",
      "PDB_wild": "1yyj",
      "MUTATED_CHAIN": "A",
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         "M7W",
         "R98I",
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      "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.",
      "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n",
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      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Bacillus caldolyticus",
      "LENGTH": 66.0,
      "UniProt": "P41016",
      "PDB_wild": "1c9o",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1c9oA00 (2.40.50.140)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Na cacodylate-HCI",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 7.22,
      "ln(ku)_H2O": -0.45,
      "dGKIN_H2O": 19.0,
      "AUTHOR_KIN": "Perl D, Welker C, Schindler T, Schr\u00f6der K, Marahiel MA, Jaenicke R, Schmid FX",
      "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9501917",
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      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Cold shock protein CspB",
      "SOURCE": "Bacillus caldolyticus",
      "LENGTH": 66.0,
      "UniProt": "P41016",
      "PDB_wild": "1c9o",
      "MUTATED_CHAIN": "A",
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         "1c9oA00 (2.40.50.140)"
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      "pH": 7.0,
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 7.22,
      "ln(ku)_H2O": -0.45,
      "dGKIN_H2O": 19.0,
      "AUTHOR_KIN": "Perl D, Welker C, Schindler T, Schr\u00f6der K, Marahiel MA, Jaenicke R, Schmid FX",
      "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9501917",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01476"
      ],
      "CATH": [
         "1e0gA00 (3.10.350.10)"
      ],
      "EC_NUMBER": "4.2.2.n1",
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      "MUTATION_PDB": "WT",
      "T": 11.0,
      "pH": 7.0,
      "BUFFER_NAME": "MOPS",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "dGKIN_H2O": 12.13,
      "mu": 5.02,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
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      "PFAM": [
         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
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      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
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      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
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   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
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      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
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      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
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      "LENGTH": 48.0,
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      "PDB_wild": "1e0g",
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      "PFAM": [
         "PF01476"
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      "CATH": [
         "1e0gA00 (3.10.350.10)"
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      "MUTATION_UNIPROT": "L434A",
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      "BUFFER_NAME": "MOPS",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "mu": 4.6,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "MUTATION_UNIPROT": "L434A",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "mu": 4.6,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "METHOD_KIN": "GdmCl",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "MUTATED_CHAIN": "A",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "MUTATION_UNIPROT": "L440M",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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      "CATH": [
         "1e0gA00 (3.10.350.10)"
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      "EC_NUMBER": "4.2.2.n1",
      "MUTATION_UNIPROT": "L440M",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "mu": 5.02,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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      "CATH": [
         "1e0gA00 (3.10.350.10)"
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      "EC_NUMBER": "4.2.2.n1",
      "MUTATION_UNIPROT": "T441A",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "mu": 4.6,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "1e0gA00 (3.10.350.10)"
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      "MUTATION_UNIPROT": "T441A",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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      "CATH": [
         "1e0gA00 (3.10.350.10)"
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      "EC_NUMBER": "4.2.2.n1",
      "MUTATION_UNIPROT": "T441S",
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      "SEC_STR": "Beta",
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      "T": 11.0,
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      "BUFFER_NAME": "MOPS",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "mu": 5.44,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
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      "MUTATED_CHAIN": "A",
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         "1e0gA00 (3.10.350.10)"
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      "EC_NUMBER": "4.2.2.n1",
      "MUTATION_UNIPROT": "T441S",
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      "BUFFER_NAME": "MOPS",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "MUTATION_UNIPROT": "L442M",
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      "SEC_STR": "Coil",
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      "BUFFER_NAME": "MOPS",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "MUTATION_UNIPROT": "L442M",
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      "METHOD_KIN": "GdmCl",
      "mu": 4.6,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
      "LENGTH": 48.0,
      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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      "CATH": [
         "1e0gA00 (3.10.350.10)"
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      "EC_NUMBER": "4.2.2.n1",
      "MUTATION_UNIPROT": "F443L",
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      "BUFFER_NAME": "MOPS",
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      "METHOD_KIN": "GdmCl",
      "mu": 5.02,
      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
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   },
   {
      "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D",
      "SOURCE": "Escherichia coli",
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      "UniProt": "P0AEZ7",
      "PDB_wild": "1e0g",
      "MUTATED_CHAIN": "A",
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         "PF01476"
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         "1e0gA00 (3.10.350.10)"
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      "EC_NUMBER": "4.2.2.n1",
      "MUTATION_UNIPROT": "F443L",
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      "BUFFER_NAME": "MOPS",
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      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J",
      "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020",
      "YEAR_KIN": 2008.0,
      "PMID_KIN": "18538343",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127G",
      "MUTATION_PDB": "D127G",
      "SEC_STR": "Helix",
      "RSA": "62.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127G",
      "MUTATION_PDB": "D127G",
      "SEC_STR": "Helix",
      "RSA": "62.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128A",
      "MUTATION_PDB": "S128A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128A",
      "MUTATION_PDB": "S128A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128G",
      "MUTATION_PDB": "S128G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128G",
      "MUTATION_PDB": "S128G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I129A",
      "MUTATION_PDB": "I129A",
      "SEC_STR": "Helix",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I129A",
      "MUTATION_PDB": "I129A",
      "SEC_STR": "Helix",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131A",
      "MUTATION_PDB": "D131A",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131A",
      "MUTATION_PDB": "D131A",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131G",
      "MUTATION_PDB": "D131G",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131G",
      "MUTATION_PDB": "D131G",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132A",
      "MUTATION_PDB": "R132A",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132A",
      "MUTATION_PDB": "R132A",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132G",
      "MUTATION_PDB": "R132G",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132G",
      "MUTATION_PDB": "R132G",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Y133A",
      "MUTATION_PDB": "Y133A",
      "SEC_STR": "Coil",
      "RSA": "31.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Y133A",
      "MUTATION_PDB": "Y133A",
      "SEC_STR": "Coil",
      "RSA": "31.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138A",
      "MUTATION_PDB": "T138A",
      "SEC_STR": "Helix",
      "RSA": "44.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138A",
      "MUTATION_PDB": "T138A",
      "SEC_STR": "Helix",
      "RSA": "44.4",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138G",
      "MUTATION_PDB": "T138G",
      "SEC_STR": "Helix",
      "RSA": "44.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138G",
      "MUTATION_PDB": "T138G",
      "SEC_STR": "Helix",
      "RSA": "44.4",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D139A",
      "MUTATION_PDB": "D139A",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D139A",
      "MUTATION_PDB": "D139A",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D139G",
      "MUTATION_PDB": "D139G",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D139G",
      "MUTATION_PDB": "D139G",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R140A",
      "MUTATION_PDB": "R140A",
      "SEC_STR": "Helix",
      "RSA": "5.2",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R140A",
      "MUTATION_PDB": "R140A",
      "SEC_STR": "Helix",
      "RSA": "5.2",
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V141A",
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      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V141A",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R142A",
      "MUTATION_PDB": "R142A",
      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R142A",
      "MUTATION_PDB": "R142A",
      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
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      "MUTATION_UNIPROT": "R142G",
      "MUTATION_PDB": "R142G",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
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      "MUTATION_PDB": "D143A",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D143G",
      "MUTATION_PDB": "D143G",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
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      "MUTATION_PDB": "D143G",
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      "BUFFER_CONC": "0.05",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S144A",
      "MUTATION_PDB": "S144A",
      "SEC_STR": "Helix",
      "RSA": "2.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 8.79,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S144A",
      "MUTATION_PDB": "S144A",
      "SEC_STR": "Helix",
      "RSA": "2.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 8.79,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L145M",
      "MUTATION_PDB": "L145M",
      "SEC_STR": "Helix",
      "RSA": "12.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L145M",
      "MUTATION_PDB": "L145M",
      "SEC_STR": "Helix",
      "RSA": "12.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146A",
      "MUTATION_PDB": "R146A",
      "SEC_STR": "Helix",
      "RSA": "60.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146A",
      "MUTATION_PDB": "R146A",
      "SEC_STR": "Helix",
      "RSA": "60.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146G",
      "MUTATION_PDB": "R146G",
      "SEC_STR": "Helix",
      "RSA": "60.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146G",
      "MUTATION_PDB": "R146G",
      "SEC_STR": "Helix",
      "RSA": "60.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W148F",
      "MUTATION_PDB": "W148F",
      "SEC_STR": "Helix",
      "RSA": "4.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W148F",
      "MUTATION_PDB": "W148F",
      "SEC_STR": "Helix",
      "RSA": "4.4",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150A",
      "MUTATION_PDB": "N150A",
      "SEC_STR": "Helix",
      "RSA": "66.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 8.37,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150A",
      "MUTATION_PDB": "N150A",
      "SEC_STR": "Helix",
      "RSA": "66.2",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150G",
      "MUTATION_PDB": "N150G",
      "SEC_STR": "Helix",
      "RSA": "66.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150G",
      "MUTATION_PDB": "N150G",
      "SEC_STR": "Helix",
      "RSA": "66.2",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "H160A",
      "MUTATION_PDB": "H160A",
      "SEC_STR": "Helix",
      "RSA": "8.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "H160A",
      "MUTATION_PDB": "H160A",
      "SEC_STR": "Helix",
      "RSA": "8.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L161A",
      "MUTATION_PDB": "L161A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L161A",
      "MUTATION_PDB": "L161A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V162A",
      "MUTATION_PDB": "V162A",
      "SEC_STR": "Helix",
      "RSA": "3.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V162A",
      "MUTATION_PDB": "V162A",
      "SEC_STR": "Helix",
      "RSA": "3.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L165A",
      "MUTATION_PDB": "L165A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L165A",
      "MUTATION_PDB": "L165A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166A",
      "MUTATION_PDB": "R166A",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166A",
      "MUTATION_PDB": "R166A",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166G",
      "MUTATION_PDB": "R166G",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166G",
      "MUTATION_PDB": "R166G",
      "SEC_STR": "Helix",
      "RSA": "48.0",
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      "BUFFER_NAME": "Phosphate",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167A",
      "MUTATION_PDB": "S167A",
      "SEC_STR": "Helix",
      "RSA": "59.2",
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167A",
      "MUTATION_PDB": "S167A",
      "SEC_STR": "Helix",
      "RSA": "59.2",
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      "BUFFER_NAME": "Phosphate",
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      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167G",
      "MUTATION_PDB": "S167G",
      "SEC_STR": "Helix",
      "RSA": "59.2",
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      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
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      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167G",
      "MUTATION_PDB": "S167G",
      "SEC_STR": "Helix",
      "RSA": "59.2",
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C168A",
      "MUTATION_PDB": "C168A",
      "SEC_STR": "Coil",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C168A",
      "MUTATION_PDB": "C168A",
      "SEC_STR": "Coil",
      "RSA": "3.0",
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      "BUFFER_NAME": "Phosphate",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V173A",
      "MUTATION_PDB": "V173A",
      "SEC_STR": "Helix",
      "RSA": "7.0",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V173A",
      "MUTATION_PDB": "V173A",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175A",
      "MUTATION_PDB": "D175A",
      "SEC_STR": "Helix",
      "RSA": "46.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175A",
      "MUTATION_PDB": "D175A",
      "SEC_STR": "Helix",
      "RSA": "46.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175G",
      "MUTATION_PDB": "D175G",
      "SEC_STR": "Helix",
      "RSA": "46.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175G",
      "MUTATION_PDB": "D175G",
      "SEC_STR": "Helix",
      "RSA": "46.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L176A",
      "MUTATION_PDB": "L176A",
      "SEC_STR": "Helix",
      "RSA": "40.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L176A",
      "MUTATION_PDB": "L176A",
      "SEC_STR": "Helix",
      "RSA": "40.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V177A",
      "MUTATION_PDB": "V177A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V177A",
      "MUTATION_PDB": "V177A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178A",
      "MUTATION_PDB": "Q178A",
      "SEC_STR": "Helix",
      "RSA": "21.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178A",
      "MUTATION_PDB": "Q178A",
      "SEC_STR": "Helix",
      "RSA": "21.7",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178G",
      "MUTATION_PDB": "Q178G",
      "SEC_STR": "Helix",
      "RSA": "21.7",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178G",
      "MUTATION_PDB": "Q178G",
      "SEC_STR": "Helix",
      "RSA": "21.7",
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V180A",
      "MUTATION_PDB": "V180A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V180A",
      "MUTATION_PDB": "V180A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98A",
      "MUTATION_PDB": "C98A",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98A",
      "MUTATION_PDB": "C98A",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.53,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98G",
      "MUTATION_PDB": "C98G",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98G",
      "MUTATION_PDB": "C98G",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "F101A",
      "MUTATION_PDB": "F101A",
      "SEC_STR": "Helix",
      "RSA": "26.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "F101A",
      "MUTATION_PDB": "F101A",
      "SEC_STR": "Helix",
      "RSA": "26.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102A",
      "MUTATION_PDB": "N102A",
      "SEC_STR": "Helix",
      "RSA": "53.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102A",
      "MUTATION_PDB": "N102A",
      "SEC_STR": "Helix",
      "RSA": "53.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102G",
      "MUTATION_PDB": "N102G",
      "SEC_STR": "Helix",
      "RSA": "53.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102G",
      "MUTATION_PDB": "N102G",
      "SEC_STR": "Helix",
      "RSA": "53.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V103A",
      "MUTATION_PDB": "V103A",
      "SEC_STR": "Helix",
      "RSA": "1.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V103A",
      "MUTATION_PDB": "V103A",
      "SEC_STR": "Helix",
      "RSA": "1.4",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I104A",
      "MUTATION_PDB": "I104A",
      "SEC_STR": "Helix",
      "RSA": "3.6",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I104A",
      "MUTATION_PDB": "I104A",
      "SEC_STR": "Helix",
      "RSA": "3.6",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W112A",
      "MUTATION_PDB": "W112A",
      "SEC_STR": "Helix",
      "RSA": "0.9",
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      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W112A",
      "MUTATION_PDB": "W112A",
      "SEC_STR": "Helix",
      "RSA": "0.9",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113A",
      "MUTATION_PDB": "R113A",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113A",
      "MUTATION_PDB": "R113A",
      "SEC_STR": "Helix",
      "RSA": "21.0",
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      "BUFFER_CONC": "0.05",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113G",
      "MUTATION_PDB": "R113G",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113G",
      "MUTATION_PDB": "R113G",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114A",
      "MUTATION_PDB": "R114A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114A",
      "MUTATION_PDB": "R114A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114G",
      "MUTATION_PDB": "R114G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114G",
      "MUTATION_PDB": "R114G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L115M",
      "MUTATION_PDB": "L115M",
      "SEC_STR": "Helix",
      "RSA": "1.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L115M",
      "MUTATION_PDB": "L115M",
      "SEC_STR": "Helix",
      "RSA": "1.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117A",
      "MUTATION_PDB": "R117A",
      "SEC_STR": "Helix",
      "RSA": "64.5",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117A",
      "MUTATION_PDB": "R117A",
      "SEC_STR": "Helix",
      "RSA": "64.5",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117G",
      "MUTATION_PDB": "R117G",
      "SEC_STR": "Helix",
      "RSA": "64.5",
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      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117G",
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      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L119M",
      "MUTATION_PDB": "L119M",
      "SEC_STR": "Helix",
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      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L119M",
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      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I126A",
      "MUTATION_PDB": "I126A",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I126A",
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      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127A",
      "MUTATION_PDB": "D127A",
      "SEC_STR": "Helix",
      "RSA": "62.0",
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      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127A",
      "MUTATION_PDB": "D127A",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "REFERENCE_KIN": "The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "2hbbA00 (3.40.5.10)"
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         "2fs1A00 (1.10.8.40)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.",
      "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Finegoldia magna",
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      "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.",
      "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109",
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      "SOURCE": "Finegoldia magna",
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      "SOURCE": "Finegoldia magna",
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      "SOURCE": "Finegoldia magna",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "PROTEIN": "PSD1(Ga88 mutant)",
      "SOURCE": "Finegoldia magna",
      "LENGTH": 50.0,
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      "MUTATED_CHAIN": "A",
      "MUTATION_UNIPROT": "T837S",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
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         "1fmkA01 (2.30.30.40)"
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      "MUTATION_UNIPROT": "I113V",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14929",
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      "PMID_KIN": "10542092",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14929",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14930",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
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         "PF00017"
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V114A",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14930",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
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         "PF00018",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14931",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
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         "PF00018",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "N115A",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14931",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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         "PF00018",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14932",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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         "PF00018",
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14932",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "G119A",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14933",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
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         "PF00018",
         "PF07714",
         "PF00017"
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "G119A",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14933",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "PFAM": [
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         "1fmkA01 (2.30.30.40)"
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14934",
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      "SOURCE": "Homo sapiens",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14934",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14935",
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      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14935",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14936",
      "YEAR_KIN": 1999.0,
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "MUTATED_CHAIN": "A",
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         "PF00018",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14936",
      "YEAR_KIN": 1999.0,
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14937",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14937",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14938",
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   {
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14938",
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   {
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14939",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14939",
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   {
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14940",
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   {
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14940",
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   {
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14941",
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   {
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14941",
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "EC_NUMBER": "2.7.10.2",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14942",
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14942",
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14943",
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14943",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14944",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "G130A",
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      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14944",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14945",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14945",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14946",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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         "1fmkA01 (2.30.30.40)"
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14946",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14947",
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   {
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14947",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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         "1fmkA01 (2.30.30.40)"
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14948",
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   {
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14948",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P12931",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14949",
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   {
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      "SOURCE": "Homo sapiens",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14949",
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   {
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14950",
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14952",
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14953",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14953",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14954",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14955",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14955",
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      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14956",
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   {
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      "MUTATION_UNIPROT": "D144A",
      "MUTATION_PDB": "D141A",
      "SEC_STR": "Coil",
      "RSA": "92.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.85,
      "mu": 2.38,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14958",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA04 (1.10.510.10)",
         "1fmkA01 (2.30.30.40)",
         "1fmkA03 (3.30.200.20)",
         "1fmkA02 (3.30.505.10)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.27,
      "mu": 2.26,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14901",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA04 (1.10.510.10)",
         "1fmkA01 (2.30.30.40)",
         "1fmkA03 (3.30.200.20)",
         "1fmkA02 (3.30.505.10)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.27,
      "mu": 2.26,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14901",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "T88A",
      "MUTATION_PDB": "T85A",
      "SEC_STR": "Beta",
      "RSA": "25.4",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.23,
      "mu": 1.92,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14902",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "T88A",
      "MUTATION_PDB": "T85A",
      "SEC_STR": "Beta",
      "RSA": "25.4",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.23,
      "mu": 1.92,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14902",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F89A",
      "MUTATION_PDB": "F86A",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.44,
      "mu": 2.13,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14903",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F89A",
      "MUTATION_PDB": "F86A",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.44,
      "mu": 2.13,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14903",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F89I",
      "MUTATION_PDB": "F86I",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.52,
      "mu": 1.84,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14904",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F89I",
      "MUTATION_PDB": "F86I",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.52,
      "mu": 1.84,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14904",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V90A",
      "MUTATION_PDB": "V87A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.56,
      "mu": 2.3,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14905",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V90A",
      "MUTATION_PDB": "V87A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.56,
      "mu": 2.3,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14905",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A91G",
      "MUTATION_PDB": "A88G",
      "SEC_STR": "Beta",
      "RSA": "1.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.52,
      "mu": 1.97,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14906",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A91G",
      "MUTATION_PDB": "A88G",
      "SEC_STR": "Beta",
      "RSA": "1.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.52,
      "mu": 1.97,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14906",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L92A",
      "MUTATION_PDB": "L89A",
      "SEC_STR": "Coil",
      "RSA": "20.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.02,
      "mu": 1.51,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14907",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L92A",
      "MUTATION_PDB": "L89A",
      "SEC_STR": "Coil",
      "RSA": "20.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.02,
      "mu": 1.51,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14907",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Y93A",
      "MUTATION_PDB": "Y90A",
      "SEC_STR": "Coil",
      "RSA": "26.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.02,
      "mu": 2.09,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14908",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Y93A",
      "MUTATION_PDB": "Y90A",
      "SEC_STR": "Coil",
      "RSA": "26.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.02,
      "mu": 2.09,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14908",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "D94A",
      "MUTATION_PDB": "D91A",
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      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14909",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "D94A",
      "MUTATION_PDB": "D91A",
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      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14909",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Y95A",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14910",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Y95A",
      "MUTATION_PDB": "Y92A",
      "SEC_STR": "Beta",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mu": 1.63,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14910",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Y95F",
      "MUTATION_PDB": "Y92F",
      "SEC_STR": "Beta",
      "RSA": "3.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.06,
      "mu": 2.72,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14911",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Y95F",
      "MUTATION_PDB": "Y92F",
      "SEC_STR": "Beta",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.06,
      "mu": 2.72,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14911",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "S97A",
      "MUTATION_PDB": "S94A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.02,
      "mu": 2.3,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14912",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
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         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "S97A",
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      "METHOD_KIN": "GuHCl",
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      "mu": 2.3,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14912",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "R98A",
      "MUTATION_PDB": "R95A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "mu": 2.55,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14913",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "R98A",
      "MUTATION_PDB": "R95A",
      "SEC_STR": "Coil",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "mu": 2.55,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14913",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "T99A",
      "MUTATION_PDB": "T96A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "mu": 2.18,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14914",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "T99A",
      "MUTATION_PDB": "T96A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.23,
      "mu": 2.18,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14914",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "T101A",
      "MUTATION_PDB": "T98A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "mu": 2.18,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14915",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "T101A",
      "MUTATION_PDB": "T98A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.18,
      "mu": 2.18,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14915",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "D102A",
      "MUTATION_PDB": "D99A",
      "SEC_STR": "Beta",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.44,
      "mu": 2.13,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14916",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "D102A",
      "MUTATION_PDB": "D99A",
      "SEC_STR": "Beta",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.44,
      "mu": 2.13,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14916",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L103A",
      "MUTATION_PDB": "L100A",
      "SEC_STR": "Coil",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.07,
      "mu": 1.88,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14917",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L103A",
      "MUTATION_PDB": "L100A",
      "SEC_STR": "Coil",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "GuHCl",
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      "mu": 1.88,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14917",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "S104A",
      "MUTATION_PDB": "S101A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.97,
      "mu": 2.43,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14918",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "S104A",
      "MUTATION_PDB": "S101A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.97,
      "mu": 2.43,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14918",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F105A",
      "MUTATION_PDB": "F102A",
      "SEC_STR": "Beta",
      "RSA": "5.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mu": 1.67,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14919",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F105A",
      "MUTATION_PDB": "F102A",
      "SEC_STR": "Beta",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mu": 1.67,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14919",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "K106A",
      "MUTATION_PDB": "K103A",
      "SEC_STR": "Coil",
      "RSA": "57.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.23,
      "mu": 2.72,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14920",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "K106A",
      "MUTATION_PDB": "K103A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.23,
      "mu": 2.72,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14920",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "K107A",
      "MUTATION_PDB": "K104A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.68,
      "mu": 2.05,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14921",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "K107A",
      "MUTATION_PDB": "K104A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -3.68,
      "mu": 2.05,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14921",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "G108A",
      "MUTATION_PDB": "G105A",
      "SEC_STR": "Coil",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.44,
      "mu": 1.8,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14922",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "G108A",
      "MUTATION_PDB": "G105A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.44,
      "mu": 1.8,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14922",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E109A",
      "MUTATION_PDB": "E106A",
      "SEC_STR": "Coil",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.56,
      "mu": 2.72,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14923",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
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      "CATH": [
         "1fmkA01 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E109A",
      "MUTATION_PDB": "E106A",
      "SEC_STR": "Coil",
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      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.56,
      "mu": 2.72,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14923",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "R110A",
      "MUTATION_PDB": "R107A",
      "SEC_STR": "Beta",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.18,
      "mu": 2.38,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14924",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "R110A",
      "MUTATION_PDB": "R107A",
      "SEC_STR": "Beta",
      "RSA": "62.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.18,
      "mu": 2.38,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14924",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L111A",
      "MUTATION_PDB": "L108A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14925",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L111A",
      "MUTATION_PDB": "L108A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14925",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L111V",
      "MUTATION_PDB": "L108V",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.31,
      "mu": 2.34,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14926",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L111V",
      "MUTATION_PDB": "L108V",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.31,
      "mu": 2.34,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14926",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Q112A",
      "MUTATION_PDB": "Q109A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.64,
      "mu": 2.3,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14927",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "Q112A",
      "MUTATION_PDB": "Q109A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -4.64,
      "mu": 2.3,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14927",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I113A",
      "MUTATION_PDB": "I110A",
      "SEC_STR": "Beta",
      "RSA": "0.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.82,
      "mu": 2.13,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14928",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "src SHR",
      "SOURCE": "Homo sapiens",
      "LENGTH": 64.0,
      "UniProt": "P12931",
      "PDB_wild": "1fmk",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018",
         "PF07714",
         "PF00017"
      ],
      "CATH": [
         "1fmkA01 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I113A",
      "MUTATION_PDB": "I110A",
      "SEC_STR": "Beta",
      "RSA": "0.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.82,
      "mu": 2.13,
      "AUTHOR_KIN": "Riddle, D.S., Grantcharova, V.P., Santiago, J.V., Alm, E., Ruczinski, I., Baker, D.",
      "REFERENCE_KIN": "Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016\u20131024. https://doi.org/10.1038/14928",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542092",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Tyrosine-protein kinase transforming protein Src",
      "SOURCE": "Rous sarcoma virus subgroup A",
      "LENGTH": 104.0,
      "UniProt": "P00524",
      "PDB_wild": "1sha",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00017"
      ],
      "CATH": [
         "1shaA00 (3.30.505.10)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "imidizole",
      "BUFFER_CONC": "0.02",
      "ADDITIVES": "0.1 mM TCEP",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.74,
      "ln(ku)_H2O": -3.48,
      "dGKIN_H2O": 29.53,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Tyrosine-protein kinase transforming protein Src",
      "SOURCE": "Rous sarcoma virus subgroup A",
      "LENGTH": 104.0,
      "UniProt": "P00524",
      "PDB_wild": "1sha",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00017"
      ],
      "CATH": [
         "1shaA00 (3.30.505.10)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "imidizole",
      "BUFFER_CONC": "0.02",
      "ADDITIVES": "0.1 mM TCEP",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.74,
      "ln(ku)_H2O": -3.48,
      "dGKIN_H2O": 29.53,
      "AUTHOR_KIN": "Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., De Los Rios, M.A., Brown, A.G., Friel, C.T., Hedberg, L., Horng, J.-C., Bona, D., Miller, E.J., Vall\u00e9e-B\u00e9lisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu, N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B., Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg, M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E., Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205428",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15689503",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "T22A",
      "MUTATION_PDB": "T21A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.3,
      "dln(kf)_H2O": -1.18,
      "ln(ku)_H2O": -6.94,
      "dln(ku)_H2O": 1.52,
      "mu": 2.28,
      "PhiF_H2O": 0.44,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205419",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "T22A",
      "MUTATION_PDB": "T21A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.3,
      "dln(kf)_H2O": -1.18,
      "ln(ku)_H2O": -6.94,
      "dln(ku)_H2O": 1.52,
      "mu": 2.28,
      "PhiF_H2O": 0.44,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205419",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "T22S",
      "MUTATION_PDB": "T21S",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.46,
      "dln(kf)_H2O": -1.34,
      "ln(ku)_H2O": -7.37,
      "dln(ku)_H2O": 1.09,
      "mu": 2.35,
      "PhiF_H2O": 0.55,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205420",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "T22S",
      "MUTATION_PDB": "T21S",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.46,
      "dln(kf)_H2O": -1.34,
      "ln(ku)_H2O": -7.37,
      "dln(ku)_H2O": 1.09,
      "mu": 2.35,
      "PhiF_H2O": 0.55,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205420",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
         "1fkbA00 (3.10.50.40)"
      ],
      "EC_NUMBER": "5.2.1.8",
      "MUTATION_UNIPROT": "I77A",
      "MUTATION_PDB": "I76A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.5,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -2.39,
      "dln(kf)_H2O": -3.27,
      "ln(ku)_H2O": -5.3,
      "dln(ku)_H2O": 3.16,
      "mu": 2.82,
      "PhiF_H2O": 0.51,
      "AUTHOR_KIN": "Fulton, K.F., Main, E.R., Daggett, V., Jackson, S.E.",
      "REFERENCE_KIN": "Protein folding: defining a \u201cstandard\u201d set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 14, 602\u2013616. https://doi.org/10.1110/ps.041205443",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10438631",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "FKBP12",
      "SOURCE": "Homo sapiens",
      "LENGTH": 107.0,
      "UniProt": "P62942",
      "PDB_wild": "1fkb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00254"
      ],
      "CATH": [
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      "REFERENCE_KIN": "Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693\u2013705. https://doi.org/10.1016/j.jmb.2005.08.054",
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      "AUTHOR_KIN": "Anil, B., Sato, S., Cho, J.-H., Raleigh, D.P.",
      "REFERENCE_KIN": "Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 354, 693\u2013705. https://doi.org/10.1016/j.jmb.2005.08.069",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Geobacillus stearothermophilus",
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      "MUTATION_UNIPROT": "L133A",
      "MUTATION_PDB": "L133A",
      "SEC_STR": "Beta",
      "RSA": "11.6",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.11,
      "dln(kf)_H2O": -3.16,
      "ln(ku)_H2O": -6.03,
      "dln(ku)_H2O": 1.82,
      "dGKIN_H2O": 15.23,
      "ddGKIN_H2O": -12.34,
      "mf": -3.47,
      "mu": 1.72,
      "PhiF_H2O": 0.63,
      "REFERENCE_KIN": "Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013\u20131021. https://doi.org/10.1021/bi061516j",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17240985",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CTL9",
      "SOURCE": "Geobacillus stearothermophilus",
      "LENGTH": 92.0,
      "UniProt": "P02417",
      "PDB_wild": "1div",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF03948"
      ],
      "CATH": [
         "1divA02 (3.10.430.100)"
      ],
      "MUTATION_UNIPROT": "H134Q",
      "MUTATION_PDB": "H134Q",
      "SEC_STR": "Beta",
      "RSA": "19.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.13,
      "dln(kf)_H2O": -2.14,
      "ln(ku)_H2O": -6.12,
      "dln(ku)_H2O": 1.73,
      "dGKIN_H2O": 18.45,
      "ddGKIN_H2O": -9.12,
      "mf": -3.47,
      "mu": 1.63,
      "PhiF_H2O": 0.55,
      "REFERENCE_KIN": "Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013\u20131021. https://doi.org/10.1021/bi061516j",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17240985",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CTL9",
      "SOURCE": "Geobacillus stearothermophilus",
      "LENGTH": 92.0,
      "UniProt": "P02417",
      "PDB_wild": "1div",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF03948"
      ],
      "CATH": [
         "1divA02 (3.10.430.100)"
      ],
      "MUTATION_UNIPROT": "H134Q",
      "MUTATION_PDB": "H134Q",
      "SEC_STR": "Beta",
      "RSA": "19.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.13,
      "dln(kf)_H2O": -2.14,
      "ln(ku)_H2O": -6.12,
      "dln(ku)_H2O": 1.73,
      "dGKIN_H2O": 18.45,
      "ddGKIN_H2O": -9.12,
      "mf": -3.47,
      "mu": 1.63,
      "PhiF_H2O": 0.55,
      "REFERENCE_KIN": "Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013\u20131021. https://doi.org/10.1021/bi061516j",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17240985",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CTL9",
      "SOURCE": "Geobacillus stearothermophilus",
      "LENGTH": 92.0,
      "UniProt": "P02417",
      "PDB_wild": "1div",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF03948"
      ],
      "CATH": [
         "1divA02 (3.10.430.100)"
      ],
      "MUTATION_UNIPROT": "V137A",
      "MUTATION_PDB": "V137A",
      "SEC_STR": "Beta",
      "RSA": "3.5",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.33,
      "dln(kf)_H2O": -1.94,
      "ln(ku)_H2O": -6.57,
      "dln(ku)_H2O": 1.28,
      "dGKIN_H2O": 19.58,
      "ddGKIN_H2O": -7.99,
      "mf": -3.22,
      "mu": 2.01,
      "PhiF_H2O": 0.6,
      "REFERENCE_KIN": "Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013\u20131021. https://doi.org/10.1021/bi061516j",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17240985",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CTL9",
      "SOURCE": "Geobacillus stearothermophilus",
      "LENGTH": 92.0,
      "UniProt": "P02417",
      "PDB_wild": "1div",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF03948"
      ],
      "CATH": [
         "1divA02 (3.10.430.100)"
      ],
      "MUTATION_UNIPROT": "V137A",
      "MUTATION_PDB": "V137A",
      "SEC_STR": "Beta",
      "RSA": "3.5",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.33,
      "dln(kf)_H2O": -1.94,
      "ln(ku)_H2O": -6.57,
      "dln(ku)_H2O": 1.28,
      "dGKIN_H2O": 19.58,
      "ddGKIN_H2O": -7.99,
      "mf": -3.22,
      "mu": 2.01,
      "PhiF_H2O": 0.6,
      "REFERENCE_KIN": "Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 46, 1013\u20131021. https://doi.org/10.1021/bi061516j",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17240985",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.1,
      "mf": -6.28,
      "mu": 2.09,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3701",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.1,
      "mf": -6.28,
      "mu": 2.09,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3701",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V41A",
      "MUTATION_PDB": "V18A",
      "SEC_STR": "Beta",
      "RSA": "23.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.7,
      "dln(kf)_H2O": -1.4,
      "mf": -5.86,
      "mu": 2.55,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3702",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V41A",
      "MUTATION_PDB": "V18A",
      "SEC_STR": "Beta",
      "RSA": "23.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.7,
      "dln(kf)_H2O": -1.4,
      "mf": -5.86,
      "mu": 2.55,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3702",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T42A",
      "MUTATION_PDB": "T19A",
      "SEC_STR": "Beta",
      "RSA": "63.4",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.28,
      "dln(kf)_H2O": -0.82,
      "mf": -6.69,
      "mu": 2.47,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3703",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T42A",
      "MUTATION_PDB": "T19A",
      "SEC_STR": "Beta",
      "RSA": "63.4",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.28,
      "dln(kf)_H2O": -0.82,
      "mf": -6.69,
      "mu": 2.47,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3703",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I43A",
      "MUTATION_PDB": "I20A",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.22,
      "dln(kf)_H2O": -2.88,
      "mf": -6.69,
      "mu": 3.22,
      "PhiF_H2O": 0.34,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3704",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I43A",
      "MUTATION_PDB": "I20A",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.22,
      "dln(kf)_H2O": -2.88,
      "mf": -6.69,
      "mu": 3.22,
      "PhiF_H2O": 0.34,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3704",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I43V",
      "MUTATION_PDB": "I20V",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.33,
      "dln(kf)_H2O": -0.77,
      "mf": -6.28,
      "mu": 2.34,
      "PhiF_H2O": 0.82,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3705",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I43V",
      "MUTATION_PDB": "I20V",
      "SEC_STR": "Beta",
      "RSA": "1.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.33,
      "dln(kf)_H2O": -0.77,
      "mf": -6.28,
      "mu": 2.34,
      "PhiF_H2O": 0.82,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3705",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K44A",
      "MUTATION_PDB": "K21A",
      "SEC_STR": "Beta",
      "RSA": "37.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.0,
      "dln(kf)_H2O": -1.1,
      "mf": -5.86,
      "mu": 2.09,
      "PhiF_H2O": 0.7,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3707",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K44A",
      "MUTATION_PDB": "K21A",
      "SEC_STR": "Beta",
      "RSA": "37.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.0,
      "dln(kf)_H2O": -1.1,
      "mf": -5.86,
      "mu": 2.09,
      "PhiF_H2O": 0.7,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3707",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A45G",
      "MUTATION_PDB": "A22G",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.34,
      "dln(kf)_H2O": -1.76,
      "mf": -7.95,
      "mu": 2.26,
      "PhiF_H2O": 0.43,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3708",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A45G",
      "MUTATION_PDB": "A22G",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.34,
      "dln(kf)_H2O": -1.76,
      "mf": -7.95,
      "mu": 2.26,
      "PhiF_H2O": 0.43,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3708",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N46A",
      "MUTATION_PDB": "N23A",
      "SEC_STR": "Beta",
      "RSA": "14.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.95,
      "dln(kf)_H2O": -0.15,
      "mf": -7.53,
      "mu": 2.34,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3709",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N46A",
      "MUTATION_PDB": "N23A",
      "SEC_STR": "Beta",
      "RSA": "14.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.95,
      "dln(kf)_H2O": -0.15,
      "mf": -7.53,
      "mu": 2.34,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3709",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L47A",
      "MUTATION_PDB": "L24A",
      "SEC_STR": "Beta",
      "RSA": "1.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.45,
      "dln(kf)_H2O": -1.65,
      "mf": -7.95,
      "mu": 2.26,
      "PhiF_H2O": 0.31,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3710",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L47A",
      "MUTATION_PDB": "L24A",
      "SEC_STR": "Beta",
      "RSA": "1.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.45,
      "dln(kf)_H2O": -1.65,
      "mf": -7.95,
      "mu": 2.26,
      "PhiF_H2O": 0.31,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3710",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I48A",
      "MUTATION_PDB": "I25A",
      "SEC_STR": "Beta",
      "RSA": "21.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.69,
      "dln(kf)_H2O": -1.41,
      "mf": -6.69,
      "mu": 2.01,
      "PhiF_H2O": 0.59,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3711",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I48A",
      "MUTATION_PDB": "I25A",
      "SEC_STR": "Beta",
      "RSA": "21.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.69,
      "dln(kf)_H2O": -1.41,
      "mf": -6.69,
      "mu": 2.01,
      "PhiF_H2O": 0.59,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3711",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I48V",
      "MUTATION_PDB": "I25V",
      "SEC_STR": "Beta",
      "RSA": "21.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.01,
      "dln(kf)_H2O": -0.09,
      "mf": -6.69,
      "mu": 2.05,
      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3712",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I48V",
      "MUTATION_PDB": "I25V",
      "SEC_STR": "Beta",
      "RSA": "21.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.01,
      "dln(kf)_H2O": -0.09,
      "mf": -6.69,
      "mu": 2.05,
      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3712",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F49A",
      "MUTATION_PDB": "F26A",
      "SEC_STR": "Coil",
      "RSA": "11.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.46,
      "dln(kf)_H2O": -0.64,
      "mf": -7.95,
      "mu": 2.34,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3714",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F49A",
      "MUTATION_PDB": "F26A",
      "SEC_STR": "Coil",
      "RSA": "11.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.46,
      "dln(kf)_H2O": -0.64,
      "mf": -7.95,
      "mu": 2.34,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3714",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F49L",
      "MUTATION_PDB": "F26L",
      "SEC_STR": "Coil",
      "RSA": "11.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.14,
      "dln(kf)_H2O": 0.04,
      "mf": -6.28,
      "mu": 2.18,
      "PhiF_H2O": -0.03,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3715",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F49L",
      "MUTATION_PDB": "F26L",
      "SEC_STR": "Coil",
      "RSA": "11.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.14,
      "dln(kf)_H2O": 0.04,
      "mf": -6.28,
      "mu": 2.18,
      "PhiF_H2O": -0.03,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3715",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A50P",
      "MUTATION_PDB": "A27P",
      "SEC_STR": "Coil",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.42,
      "dln(kf)_H2O": 0.32,
      "mf": -6.28,
      "mu": 2.34,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3717",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A50P",
      "MUTATION_PDB": "A27P",
      "SEC_STR": "Coil",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.42,
      "dln(kf)_H2O": 0.32,
      "mf": -6.28,
      "mu": 2.34,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3717",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A50V",
      "MUTATION_PDB": "A27V",
      "SEC_STR": "Coil",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.0,
      "dln(kf)_H2O": -1.1,
      "mf": -7.11,
      "mu": 2.47,
      "PhiF_H2O": 0.78,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3718",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A50V",
      "MUTATION_PDB": "A27V",
      "SEC_STR": "Coil",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.0,
      "dln(kf)_H2O": -1.1,
      "mf": -7.11,
      "mu": 2.47,
      "PhiF_H2O": 0.78,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3718",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N51A",
      "MUTATION_PDB": "N28A",
      "SEC_STR": "Coil",
      "RSA": "73.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.0,
      "dln(kf)_H2O": -2.1,
      "mf": -7.11,
      "mu": 2.3,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3719",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N51A",
      "MUTATION_PDB": "N28A",
      "SEC_STR": "Coil",
      "RSA": "73.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.0,
      "dln(kf)_H2O": -2.1,
      "mf": -7.11,
      "mu": 2.3,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3719",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G52A",
      "MUTATION_PDB": "G29A",
      "SEC_STR": "Coil",
      "RSA": "70.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.96,
      "dln(kf)_H2O": -2.14,
      "mf": -7.53,
      "mu": 2.43,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3720",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G52A",
      "MUTATION_PDB": "G29A",
      "SEC_STR": "Coil",
      "RSA": "70.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.96,
      "dln(kf)_H2O": -2.14,
      "mf": -7.53,
      "mu": 2.43,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3720",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G52V",
      "MUTATION_PDB": "G29V",
      "SEC_STR": "Coil",
      "RSA": "70.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.45,
      "dln(kf)_H2O": -2.65,
      "mf": -7.53,
      "mu": 2.43,
      "PhiF_H2O": 0.61,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3721",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G52V",
      "MUTATION_PDB": "G29V",
      "SEC_STR": "Coil",
      "RSA": "70.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.45,
      "dln(kf)_H2O": -2.65,
      "mf": -7.53,
      "mu": 2.43,
      "PhiF_H2O": 0.61,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3721",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N51A,G52A",
      "MUTATION_PDB": "N28A,G29A",
      "SEC_STR": "Coil,Coil",
      "RSA": "73.9,70.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.05,
      "dln(kf)_H2O": -3.05,
      "mf": -7.95,
      "mu": 2.18,
      "PhiF_H2O": 0.65,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3724",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N51A,G52A",
      "MUTATION_PDB": "N28A,G29A",
      "SEC_STR": "Coil,Coil",
      "RSA": "73.9,70.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.05,
      "dln(kf)_H2O": -3.05,
      "mf": -7.95,
      "mu": 2.18,
      "PhiF_H2O": 0.65,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3724",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "S53A",
      "MUTATION_PDB": "S30A",
      "SEC_STR": "Coil",
      "RSA": "46.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": 0.1,
      "mf": -6.69,
      "mu": 2.13,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3725",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "S53A",
      "MUTATION_PDB": "S30A",
      "SEC_STR": "Coil",
      "RSA": "46.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": 0.1,
      "mf": -6.69,
      "mu": 2.13,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3725",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T54A",
      "MUTATION_PDB": "T31A",
      "SEC_STR": "Coil",
      "RSA": "63.4",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.28,
      "dln(kf)_H2O": -0.82,
      "mf": -6.69,
      "mu": 2.26,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3726",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T54A",
      "MUTATION_PDB": "T31A",
      "SEC_STR": "Coil",
      "RSA": "63.4",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.28,
      "dln(kf)_H2O": -0.82,
      "mf": -6.69,
      "mu": 2.26,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3726",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T56A",
      "MUTATION_PDB": "T33A",
      "SEC_STR": "Beta",
      "RSA": "47.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.79,
      "dln(kf)_H2O": -0.31,
      "mf": -6.69,
      "mu": 2.43,
      "PhiF_H2O": 0.17,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3727",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T56A",
      "MUTATION_PDB": "T33A",
      "SEC_STR": "Beta",
      "RSA": "47.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.79,
      "dln(kf)_H2O": -0.31,
      "mf": -6.69,
      "mu": 2.43,
      "PhiF_H2O": 0.17,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3727",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A57G",
      "MUTATION_PDB": "A34G",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.95,
      "dln(kf)_H2O": -1.15,
      "mf": -7.11,
      "mu": 2.43,
      "PhiF_H2O": 0.31,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3728",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A57G",
      "MUTATION_PDB": "A34G",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.95,
      "dln(kf)_H2O": -1.15,
      "mf": -7.11,
      "mu": 2.43,
      "PhiF_H2O": 0.31,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3728",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A57V",
      "MUTATION_PDB": "A34V",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.48,
      "dln(kf)_H2O": 1.38,
      "mf": -5.02,
      "mu": 2.26,
      "PhiF_H2O": 0.54,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3729",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A57V",
      "MUTATION_PDB": "A34V",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.48,
      "dln(kf)_H2O": 1.38,
      "mf": -5.02,
      "mu": 2.26,
      "PhiF_H2O": 0.54,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3729",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E58A",
      "MUTATION_PDB": "E35A",
      "SEC_STR": "Beta",
      "RSA": "69.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.03,
      "dln(kf)_H2O": -1.07,
      "mf": -5.86,
      "mu": 18.95,
      "PhiF_H2O": 1.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3730",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E58A",
      "MUTATION_PDB": "E35A",
      "SEC_STR": "Beta",
      "RSA": "69.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.03,
      "dln(kf)_H2O": -1.07,
      "mf": -5.86,
      "mu": 18.95,
      "PhiF_H2O": 1.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3730",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F59A",
      "MUTATION_PDB": "F36A",
      "SEC_STR": "Beta",
      "RSA": "8.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 0.82,
      "dln(kf)_H2O": -3.28,
      "mf": -7.11,
      "mu": 3.39,
      "PhiF_H2O": 0.45,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3731",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F59A",
      "MUTATION_PDB": "F36A",
      "SEC_STR": "Beta",
      "RSA": "8.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 0.82,
      "dln(kf)_H2O": -3.28,
      "mf": -7.11,
      "mu": 3.39,
      "PhiF_H2O": 0.45,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3731",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F59L",
      "MUTATION_PDB": "F36L",
      "SEC_STR": "Beta",
      "RSA": "8.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.75,
      "dln(kf)_H2O": -1.35,
      "mf": -7.53,
      "mu": 2.89,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3732",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F59L",
      "MUTATION_PDB": "F36L",
      "SEC_STR": "Beta",
      "RSA": "8.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.75,
      "dln(kf)_H2O": -1.35,
      "mf": -7.53,
      "mu": 2.89,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3732",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K60A",
      "MUTATION_PDB": "K37A",
      "SEC_STR": "Beta",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.25,
      "dln(kf)_H2O": -0.85,
      "mf": -6.28,
      "mu": 2.13,
      "PhiF_H2O": 0.57,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3734",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K60A",
      "MUTATION_PDB": "K37A",
      "SEC_STR": "Beta",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.25,
      "dln(kf)_H2O": -0.85,
      "mf": -6.28,
      "mu": 2.13,
      "PhiF_H2O": 0.57,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3734",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G61A",
      "MUTATION_PDB": "G38A",
      "SEC_STR": "Beta",
      "RSA": "27.4",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.38,
      "dln(kf)_H2O": -0.72,
      "mf": -7.11,
      "mu": 2.43,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3735",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G61A",
      "MUTATION_PDB": "G38A",
      "SEC_STR": "Beta",
      "RSA": "27.4",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.38,
      "dln(kf)_H2O": -0.72,
      "mf": -7.11,
      "mu": 2.43,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3735",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T62A",
      "MUTATION_PDB": "T39A",
      "SEC_STR": "Coil",
      "RSA": "55.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.32,
      "dln(kf)_H2O": -0.78,
      "mf": -5.86,
      "mu": 2.22,
      "PhiF_H2O": 0.37,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3736",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T62A",
      "MUTATION_PDB": "T39A",
      "SEC_STR": "Coil",
      "RSA": "55.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.32,
      "dln(kf)_H2O": -0.78,
      "mf": -5.86,
      "mu": 2.22,
      "PhiF_H2O": 0.37,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3736",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F63G",
      "MUTATION_PDB": "F40G",
      "SEC_STR": "Coil",
      "RSA": "39.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.06,
      "dln(kf)_H2O": -1.04,
      "mf": -7.95,
      "mu": 2.64,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3737",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F63G",
      "MUTATION_PDB": "F40G",
      "SEC_STR": "Coil",
      "RSA": "39.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.06,
      "dln(kf)_H2O": -1.04,
      "mf": -7.95,
      "mu": 2.64,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3737",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F63L",
      "MUTATION_PDB": "F40L",
      "SEC_STR": "Coil",
      "RSA": "39.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.95,
      "dln(kf)_H2O": -0.15,
      "mf": -5.86,
      "mu": 2.26,
      "PhiF_H2O": 0.24,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3738",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F63L",
      "MUTATION_PDB": "F40L",
      "SEC_STR": "Coil",
      "RSA": "39.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.95,
      "dln(kf)_H2O": -0.15,
      "mf": -5.86,
      "mu": 2.26,
      "PhiF_H2O": 0.24,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3738",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K65G",
      "MUTATION_PDB": "K42G",
      "SEC_STR": "Helix",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.85,
      "dln(kf)_H2O": -0.25,
      "mf": -5.44,
      "mu": 2.09,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3740",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K65G",
      "MUTATION_PDB": "K42G",
      "SEC_STR": "Helix",
      "RSA": "56.6",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.85,
      "dln(kf)_H2O": -0.25,
      "mf": -5.44,
      "mu": 2.09,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3740",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A66G",
      "MUTATION_PDB": "A43G",
      "SEC_STR": "Helix",
      "RSA": "3.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.23,
      "dln(kf)_H2O": -0.87,
      "mf": -6.69,
      "mu": 2.18,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3741",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A66G",
      "MUTATION_PDB": "A43G",
      "SEC_STR": "Helix",
      "RSA": "3.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.23,
      "dln(kf)_H2O": -0.87,
      "mf": -6.69,
      "mu": 2.18,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3741",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T67A",
      "MUTATION_PDB": "T44A",
      "SEC_STR": "Helix",
      "RSA": "21.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.85,
      "dln(kf)_H2O": -0.25,
      "mf": -5.86,
      "mu": 2.55,
      "PhiF_H2O": 0.14,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3742",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T67A",
      "MUTATION_PDB": "T44A",
      "SEC_STR": "Helix",
      "RSA": "21.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.85,
      "dln(kf)_H2O": -0.25,
      "mf": -5.86,
      "mu": 2.55,
      "PhiF_H2O": 0.14,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3742",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "S68A",
      "MUTATION_PDB": "S45A",
      "SEC_STR": "Helix",
      "RSA": "50.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.47,
      "dln(kf)_H2O": 0.37,
      "mf": -6.28,
      "mu": 2.3,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3743",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "S68A",
      "MUTATION_PDB": "S45A",
      "SEC_STR": "Helix",
      "RSA": "50.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.47,
      "dln(kf)_H2O": 0.37,
      "mf": -6.28,
      "mu": 2.3,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3743",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "S68G",
      "MUTATION_PDB": "S45G",
      "SEC_STR": "Helix",
      "RSA": "50.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.05,
      "dln(kf)_H2O": -0.05,
      "mf": -7.11,
      "mu": 2.3,
      "PhiF_H2O": 0.04,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3744",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "S68G",
      "MUTATION_PDB": "S45G",
      "SEC_STR": "Helix",
      "RSA": "50.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.05,
      "dln(kf)_H2O": -0.05,
      "mf": -7.11,
      "mu": 2.3,
      "PhiF_H2O": 0.04,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3744",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E69G",
      "MUTATION_PDB": "E46G",
      "SEC_STR": "Helix",
      "RSA": "49.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.88,
      "dln(kf)_H2O": -0.22,
      "mf": -6.28,
      "mu": 2.38,
      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3746",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E69G",
      "MUTATION_PDB": "E46G",
      "SEC_STR": "Helix",
      "RSA": "49.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.88,
      "dln(kf)_H2O": -0.22,
      "mf": -6.28,
      "mu": 2.38,
      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3746",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E69I",
      "MUTATION_PDB": "E46I",
      "SEC_STR": "Helix",
      "RSA": "49.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.01,
      "dln(kf)_H2O": -0.09,
      "mf": -6.28,
      "mu": 2.64,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3747",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E69I",
      "MUTATION_PDB": "E46I",
      "SEC_STR": "Helix",
      "RSA": "49.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.01,
      "dln(kf)_H2O": -0.09,
      "mf": -6.28,
      "mu": 2.64,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3747",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A70G",
      "MUTATION_PDB": "A47G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.2,
      "dln(kf)_H2O": -0.9,
      "mf": -8.37,
      "mu": 2.51,
      "PhiF_H2O": 0.17,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3748",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A70G",
      "MUTATION_PDB": "A47G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.2,
      "dln(kf)_H2O": -0.9,
      "mf": -8.37,
      "mu": 2.51,
      "PhiF_H2O": 0.17,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3748",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y71A",
      "MUTATION_PDB": "Y48A",
      "SEC_STR": "Helix",
      "RSA": "48.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.28,
      "dln(kf)_H2O": 0.18,
      "mf": -8.79,
      "mu": 2.51,
      "PhiF_H2O": -0.04,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3749",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y71A",
      "MUTATION_PDB": "Y48A",
      "SEC_STR": "Helix",
      "RSA": "48.2",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.28,
      "dln(kf)_H2O": 0.18,
      "mf": -8.79,
      "mu": 2.51,
      "PhiF_H2O": -0.04,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3749",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A72G",
      "MUTATION_PDB": "A49G",
      "SEC_STR": "Helix",
      "RSA": "55.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.52,
      "dln(kf)_H2O": -0.58,
      "mf": -6.28,
      "mu": 2.09,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3750",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A72G",
      "MUTATION_PDB": "A49G",
      "SEC_STR": "Helix",
      "RSA": "55.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.52,
      "dln(kf)_H2O": -0.58,
      "mf": -6.28,
      "mu": 2.09,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3750",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y73A",
      "MUTATION_PDB": "Y50A",
      "SEC_STR": "Helix",
      "RSA": "45.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.94,
      "dln(kf)_H2O": -1.16,
      "mf": -6.28,
      "mu": 2.55,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3751",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y73A",
      "MUTATION_PDB": "Y50A",
      "SEC_STR": "Helix",
      "RSA": "45.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.94,
      "dln(kf)_H2O": -1.16,
      "mf": -6.28,
      "mu": 2.55,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3751",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A74G",
      "MUTATION_PDB": "A51G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.71,
      "dln(kf)_H2O": -0.39,
      "mf": -7.53,
      "mu": 2.89,
      "PhiF_H2O": 0.07,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3752",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A74G",
      "MUTATION_PDB": "A51G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.71,
      "dln(kf)_H2O": -0.39,
      "mf": -7.53,
      "mu": 2.89,
      "PhiF_H2O": 0.07,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3752",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D75A",
      "MUTATION_PDB": "D52A",
      "SEC_STR": "Helix",
      "RSA": "55.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.86,
      "dln(kf)_H2O": 0.76,
      "mf": -6.69,
      "mu": 2.26,
      "PhiF_H2O": -0.42,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3753",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D75A",
      "MUTATION_PDB": "D52A",
      "SEC_STR": "Helix",
      "RSA": "55.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.86,
      "dln(kf)_H2O": 0.76,
      "mf": -6.69,
      "mu": 2.26,
      "PhiF_H2O": -0.42,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3753",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D75G",
      "MUTATION_PDB": "D52G",
      "SEC_STR": "Helix",
      "RSA": "55.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.4,
      "dln(kf)_H2O": 0.3,
      "mf": -7.11,
      "mu": 2.34,
      "PhiF_H2O": -0.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3754",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D75G",
      "MUTATION_PDB": "D52G",
      "SEC_STR": "Helix",
      "RSA": "55.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.4,
      "dln(kf)_H2O": 0.3,
      "mf": -7.11,
      "mu": 2.34,
      "PhiF_H2O": -0.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3754",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T76G",
      "MUTATION_PDB": "T53G",
      "SEC_STR": "Coil",
      "RSA": "80.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.69,
      "dln(kf)_H2O": 0.59,
      "mf": -6.28,
      "mu": 2.51,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3756",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T76G",
      "MUTATION_PDB": "T53G",
      "SEC_STR": "Coil",
      "RSA": "80.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.69,
      "dln(kf)_H2O": 0.59,
      "mf": -6.28,
      "mu": 2.51,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3756",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L77A",
      "MUTATION_PDB": "L54A",
      "SEC_STR": "Coil",
      "RSA": "28.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.78,
      "dln(kf)_H2O": -0.32,
      "mf": -7.11,
      "mu": 2.18,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3757",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L77A",
      "MUTATION_PDB": "L54A",
      "SEC_STR": "Coil",
      "RSA": "28.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.78,
      "dln(kf)_H2O": -0.32,
      "mf": -7.11,
      "mu": 2.18,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3757",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E69G,A72G,T76G",
      "MUTATION_PDB": "E46G,A49G,T53G",
      "SEC_STR": "Helix,Helix,Coil",
      "RSA": "49.5,55.7,80.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.22,
      "dln(kf)_H2O": -0.88,
      "mf": -7.53,
      "mu": 2.8,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3758",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E69G,A72G,T76G",
      "MUTATION_PDB": "E46G,A49G,T53G",
      "SEC_STR": "Helix,Helix,Coil",
      "RSA": "49.5,55.7,80.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.22,
      "dln(kf)_H2O": -0.88,
      "mf": -7.53,
      "mu": 2.8,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3758",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K78A",
      "MUTATION_PDB": "K55A",
      "SEC_STR": "Coil",
      "RSA": "44.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.23,
      "dln(kf)_H2O": 0.13,
      "mf": -5.86,
      "mu": 1.97,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3759",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K78A",
      "MUTATION_PDB": "K55A",
      "SEC_STR": "Coil",
      "RSA": "44.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.23,
      "dln(kf)_H2O": 0.13,
      "mf": -5.86,
      "mu": 1.97,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3759",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K79A",
      "MUTATION_PDB": "K56A",
      "SEC_STR": "Coil",
      "RSA": "82.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.11,
      "dln(kf)_H2O": 0.01,
      "mf": -5.86,
      "mu": 2.26,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3760",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K79A",
      "MUTATION_PDB": "K56A",
      "SEC_STR": "Coil",
      "RSA": "82.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.11,
      "dln(kf)_H2O": 0.01,
      "mf": -5.86,
      "mu": 2.26,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3760",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N81A",
      "MUTATION_PDB": "N58A",
      "SEC_STR": "Coil",
      "RSA": "25.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.06,
      "dln(kf)_H2O": -0.04,
      "mf": -6.28,
      "mu": 2.05,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3761",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N81A",
      "MUTATION_PDB": "N58A",
      "SEC_STR": "Coil",
      "RSA": "25.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.06,
      "dln(kf)_H2O": -0.04,
      "mf": -6.28,
      "mu": 2.05,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3761",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G82A",
      "MUTATION_PDB": "G59A",
      "SEC_STR": "Coil",
      "RSA": "59.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.5,
      "dln(kf)_H2O": 0.4,
      "mf": -7.11,
      "mu": 1.88,
      "PhiF_H2O": -0.1,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3762",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G82A",
      "MUTATION_PDB": "G59A",
      "SEC_STR": "Coil",
      "RSA": "59.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.5,
      "dln(kf)_H2O": 0.4,
      "mf": -7.11,
      "mu": 1.88,
      "PhiF_H2O": -0.1,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3762",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E83A",
      "MUTATION_PDB": "E60A",
      "SEC_STR": "Coil",
      "RSA": "57.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.11,
      "dln(kf)_H2O": 0.01,
      "mf": -6.28,
      "mu": 2.26,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3763",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E83A",
      "MUTATION_PDB": "E60A",
      "SEC_STR": "Coil",
      "RSA": "57.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.11,
      "dln(kf)_H2O": 0.01,
      "mf": -6.28,
      "mu": 2.26,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3763",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T85A",
      "MUTATION_PDB": "T62A",
      "SEC_STR": "Beta",
      "RSA": "62.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.31,
      "dln(kf)_H2O": -0.79,
      "mf": -5.86,
      "mu": 2.8,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3764",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T85A",
      "MUTATION_PDB": "T62A",
      "SEC_STR": "Beta",
      "RSA": "62.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.31,
      "dln(kf)_H2O": -0.79,
      "mf": -5.86,
      "mu": 2.8,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3764",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V86A",
      "MUTATION_PDB": "V63A",
      "SEC_STR": "Beta",
      "RSA": "33.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.55,
      "dln(kf)_H2O": -0.55,
      "mf": -6.28,
      "mu": 2.26,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3765",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V86A",
      "MUTATION_PDB": "V63A",
      "SEC_STR": "Beta",
      "RSA": "33.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.55,
      "dln(kf)_H2O": -0.55,
      "mf": -6.28,
      "mu": 2.26,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3765",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D87A",
      "MUTATION_PDB": "D64A",
      "SEC_STR": "Coil",
      "RSA": "52.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.43,
      "dln(kf)_H2O": 0.33,
      "mf": -6.28,
      "mu": 2.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3766",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D87A",
      "MUTATION_PDB": "D64A",
      "SEC_STR": "Coil",
      "RSA": "52.1",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.43,
      "dln(kf)_H2O": 0.33,
      "mf": -6.28,
      "mu": 2.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3766",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V88A",
      "MUTATION_PDB": "V65A",
      "SEC_STR": "Coil",
      "RSA": "71.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.84,
      "dln(kf)_H2O": -0.26,
      "mf": -6.28,
      "mu": 2.22,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3767",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V88A",
      "MUTATION_PDB": "V65A",
      "SEC_STR": "Coil",
      "RSA": "71.8",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.84,
      "dln(kf)_H2O": -0.26,
      "mf": -6.28,
      "mu": 2.22,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3767",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A89G",
      "MUTATION_PDB": "A66G",
      "SEC_STR": "Beta",
      "RSA": "44.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.08,
      "dln(kf)_H2O": -0.02,
      "mf": -5.44,
      "mu": 2.26,
      "PhiF_H2O": 0.04,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3768",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A89G",
      "MUTATION_PDB": "A66G",
      "SEC_STR": "Beta",
      "RSA": "44.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.08,
      "dln(kf)_H2O": -0.02,
      "mf": -5.44,
      "mu": 2.26,
      "PhiF_H2O": 0.04,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3768",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K91A",
      "MUTATION_PDB": "K68A",
      "SEC_STR": "Coil",
      "RSA": "83.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": 0.1,
      "mf": -6.28,
      "mu": 2.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3769",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K91A",
      "MUTATION_PDB": "K68A",
      "SEC_STR": "Coil",
      "RSA": "83.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": 0.1,
      "mf": -6.28,
      "mu": 2.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3769",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G92A",
      "MUTATION_PDB": "G69A",
      "SEC_STR": "Coil",
      "RSA": "33.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.57,
      "dln(kf)_H2O": -0.53,
      "mf": -7.53,
      "mu": 2.64,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3770",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G92A",
      "MUTATION_PDB": "G69A",
      "SEC_STR": "Coil",
      "RSA": "33.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.57,
      "dln(kf)_H2O": -0.53,
      "mf": -7.53,
      "mu": 2.64,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3770",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y93A",
      "MUTATION_PDB": "Y70A",
      "SEC_STR": "Coil",
      "RSA": "2.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.93,
      "dln(kf)_H2O": -0.17,
      "mf": -7.53,
      "mu": 2.09,
      "PhiF_H2O": 0.06,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3771",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y93A",
      "MUTATION_PDB": "Y70A",
      "SEC_STR": "Coil",
      "RSA": "2.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.93,
      "dln(kf)_H2O": -0.17,
      "mf": -7.53,
      "mu": 2.09,
      "PhiF_H2O": 0.06,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3771",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y93L",
      "MUTATION_PDB": "Y70L",
      "SEC_STR": "Coil",
      "RSA": "2.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.62,
      "dln(kf)_H2O": -0.48,
      "mf": -5.86,
      "mu": 1.97,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3772",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y93L",
      "MUTATION_PDB": "Y70L",
      "SEC_STR": "Coil",
      "RSA": "2.3",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.62,
      "dln(kf)_H2O": -0.48,
      "mf": -5.86,
      "mu": 1.97,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3772",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T94A",
      "MUTATION_PDB": "T71A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.88,
      "dln(kf)_H2O": -0.22,
      "mf": -7.11,
      "mu": 2.22,
      "PhiF_H2O": 0.07,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3774",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T94A",
      "MUTATION_PDB": "T71A",
      "SEC_STR": "Beta",
      "RSA": "19.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.88,
      "dln(kf)_H2O": -0.22,
      "mf": -7.11,
      "mu": 2.22,
      "PhiF_H2O": 0.07,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3774",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L95A",
      "MUTATION_PDB": "L72A",
      "SEC_STR": "Beta",
      "RSA": "3.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.4,
      "dln(kf)_H2O": -1.7,
      "mf": -6.28,
      "mu": 2.89,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3775",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L95A",
      "MUTATION_PDB": "L72A",
      "SEC_STR": "Beta",
      "RSA": "3.7",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.4,
      "dln(kf)_H2O": -1.7,
      "mf": -6.28,
      "mu": 2.89,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3775",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N96A",
      "MUTATION_PDB": "N73A",
      "SEC_STR": "Beta",
      "RSA": "28.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.75,
      "dln(kf)_H2O": -0.35,
      "mf": -6.69,
      "mu": 2.09,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3776",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N96A",
      "MUTATION_PDB": "N73A",
      "SEC_STR": "Beta",
      "RSA": "28.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.75,
      "dln(kf)_H2O": -0.35,
      "mf": -6.69,
      "mu": 2.09,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3776",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I97A",
      "MUTATION_PDB": "I74A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.24,
      "dln(kf)_H2O": -1.86,
      "mf": -3.35,
      "mu": 3.35,
      "PhiF_H2O": 0.23,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3777",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I97A",
      "MUTATION_PDB": "I74A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.24,
      "dln(kf)_H2O": -1.86,
      "mf": -3.35,
      "mu": 3.35,
      "PhiF_H2O": 0.23,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3777",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I97V",
      "MUTATION_PDB": "I74V",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.62,
      "dln(kf)_H2O": -0.48,
      "mf": -6.69,
      "mu": 2.47,
      "PhiF_H2O": 0.17,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3778",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I97V",
      "MUTATION_PDB": "I74V",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.62,
      "dln(kf)_H2O": -0.48,
      "mf": -6.69,
      "mu": 2.47,
      "PhiF_H2O": 0.17,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3778",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K98A",
      "MUTATION_PDB": "K75A",
      "SEC_STR": "Beta",
      "RSA": "45.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.97,
      "dln(kf)_H2O": -0.13,
      "mf": -6.28,
      "mu": 2.09,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3780",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K98A",
      "MUTATION_PDB": "K75A",
      "SEC_STR": "Beta",
      "RSA": "45.9",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.97,
      "dln(kf)_H2O": -0.13,
      "mf": -6.28,
      "mu": 2.09,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3780",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F99L",
      "MUTATION_PDB": "F76L",
      "SEC_STR": "Beta",
      "RSA": "0.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.03,
      "dln(kf)_H2O": -0.07,
      "mf": -6.69,
      "mu": 2.55,
      "PhiF_H2O": 0.01,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3781",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F99L",
      "MUTATION_PDB": "F76L",
      "SEC_STR": "Beta",
      "RSA": "0.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.03,
      "dln(kf)_H2O": -0.07,
      "mf": -6.69,
      "mu": 2.55,
      "PhiF_H2O": 0.01,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3781",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F99V",
      "MUTATION_PDB": "F76V",
      "SEC_STR": "Beta",
      "RSA": "0.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": 0.1,
      "mf": -6.28,
      "mu": 3.1,
      "PhiF_H2O": -0.02,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3782",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein LG",
      "SOURCE": "Finegoldia magna (Peptostreptococcus magnus)",
      "LENGTH": 78.0,
      "UniProt": "Q53291",
      "PDB_wild": "2ptl",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02246"
      ],
      "CATH": [
         "2ptlA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F99V",
      "MUTATION_PDB": "F76V",
      "SEC_STR": "Beta",
      "RSA": "0.5",
      "T": 22.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": 0.1,
      "mf": -6.28,
      "mu": 3.1,
      "PhiF_H2O": -0.02,
      "AUTHOR_KIN": "Kim, D.E., Fisher, C., Baker, D.",
      "REFERENCE_KIN": "A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971\u2013984. https://doi.org/10.1006/jmbi.2000.3782",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10801362",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.23,
      "mu": 2.03,
      "beta-T": 0.72,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.23,
      "mu": 2.03,
      "beta-T": 0.72,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107D",
      "MUTATION_PDB": "E107D",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.62,
      "mu": 1.68,
      "beta-T": 0.77,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107D",
      "MUTATION_PDB": "E107D",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.62,
      "mu": 1.68,
      "beta-T": 0.77,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107Q",
      "MUTATION_PDB": "E107Q",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.52,
      "mu": 2.16,
      "beta-T": 0.72,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107Q",
      "MUTATION_PDB": "E107Q",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.52,
      "mu": 2.16,
      "beta-T": 0.72,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107T",
      "MUTATION_PDB": "E107T",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.52,
      "mu": 1.81,
      "beta-T": 0.78,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107T",
      "MUTATION_PDB": "E107T",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.52,
      "mu": 1.81,
      "beta-T": 0.78,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107H",
      "MUTATION_PDB": "E107H",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.87,
      "mu": 1.91,
      "beta-T": 0.75,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107H",
      "MUTATION_PDB": "E107H",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.87,
      "mu": 1.91,
      "beta-T": 0.75,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107K",
      "MUTATION_PDB": "E107K",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.18,
      "mu": 2.16,
      "beta-T": 0.71,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107K",
      "MUTATION_PDB": "E107K",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.18,
      "mu": 2.16,
      "beta-T": 0.71,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107A",
      "MUTATION_PDB": "E107A",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.7,
      "mu": 1.68,
      "beta-T": 0.77,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107A",
      "MUTATION_PDB": "E107A",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.7,
      "mu": 1.68,
      "beta-T": 0.77,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107S",
      "MUTATION_PDB": "E107S",
      "SEC_STR": "Coil",
      "RSA": "10.3",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.25,
      "mu": 2.28,
      "beta-T": 0.7,
      "AUTHOR_KIN": "Northey JGB, Maxwell KL, Davidson AR",
      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "12079394",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "E107S",
      "MUTATION_PDB": "E107S",
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      "PMID_KIN": "12079394",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1shfA00 (2.30.30.40)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 62.0,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06241",
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      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J Mol Biol 320(2):389-402. https://doi.org/10.1016/S0022-2836(02)00445-X",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.41,
      "ln(ku)_H2O": -0.67,
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      "mu": 3.43,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb748",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb748",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P06241",
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      "MUTATED_CHAIN": "A",
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         "1shfA00 (2.30.30.40)"
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      "MUTATION_UNIPROT": "F87S",
      "MUTATION_PDB": "F87S",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
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      "MEASURE_KIN": "stopped-flow",
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      "dln(ku)_H2O": 2.62,
      "ddGKIN_H2O": -8.2,
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      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb749",
      "YEAR_KIN": 2002.0,
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
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      "MUTATED_CHAIN": "A",
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      "MUTATION_UNIPROT": "F87S",
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      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb749",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
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      "UniProt": "P06241",
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         "1shfA00 (2.30.30.40)"
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      "MUTATION_UNIPROT": "F87A",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06241",
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P06241",
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      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb751",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F87V",
      "MUTATION_PDB": "F87V",
      "SEC_STR": "Beta",
      "RSA": "17.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.17,
      "dln(kf)_H2O": -0.24,
      "ln(ku)_H2O": -0.13,
      "dln(ku)_H2O": 0.54,
      "ddGKIN_H2O": -1.97,
      "mf": -8.58,
      "mu": 3.18,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb751",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F87L",
      "MUTATION_PDB": "F87L",
      "SEC_STR": "Beta",
      "RSA": "17.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.97,
      "dln(kf)_H2O": -0.44,
      "ln(ku)_H2O": 2.25,
      "dln(ku)_H2O": 2.92,
      "ddGKIN_H2O": -8.33,
      "mf": -8.37,
      "mu": 3.64,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb752",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F87L",
      "MUTATION_PDB": "F87L",
      "SEC_STR": "Beta",
      "RSA": "17.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.97,
      "dln(kf)_H2O": -0.44,
      "ln(ku)_H2O": 2.25,
      "dln(ku)_H2O": 2.92,
      "ddGKIN_H2O": -8.33,
      "mf": -8.37,
      "mu": 3.64,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb752",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A89S",
      "MUTATION_PDB": "A89S",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.1,
      "dln(kf)_H2O": -0.31,
      "ln(ku)_H2O": 1.16,
      "dln(ku)_H2O": 1.83,
      "ddGKIN_H2O": -5.27,
      "mf": -7.91,
      "mu": 4.31,
      "PhiF_H2O": 0.14,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb753",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A89S",
      "MUTATION_PDB": "A89S",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.1,
      "dln(kf)_H2O": -0.31,
      "ln(ku)_H2O": 1.16,
      "dln(ku)_H2O": 1.83,
      "ddGKIN_H2O": -5.27,
      "mf": -7.91,
      "mu": 4.31,
      "PhiF_H2O": 0.14,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb753",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A89G",
      "MUTATION_PDB": "A89G",
      "SEC_STR": "Beta",
      "RSA": "2.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.92,
      "dln(kf)_H2O": -0.49,
      "ln(ku)_H2O": 1.48,
      "dln(ku)_H2O": 2.15,
      "ddGKIN_H2O": -6.53,
      "mf": -8.37,
      "mu": 2.8,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb754",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A89G",
      "MUTATION_PDB": "A89G",
      "SEC_STR": "Beta",
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      "T": 25.0,
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.92,
      "dln(kf)_H2O": -0.49,
      "ln(ku)_H2O": 1.48,
      "dln(ku)_H2O": 2.15,
      "ddGKIN_H2O": -6.53,
      "mf": -8.37,
      "mu": 2.8,
      "PhiF_H2O": 0.18,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb754",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A89L,F103L",
      "MUTATION_PDB": "A89L,F103L",
      "SEC_STR": "Beta,Beta",
      "RSA": "2.8,2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.95,
      "dln(kf)_H2O": 0.54,
      "ln(ku)_H2O": 4.52,
      "dln(ku)_H2O": 5.19,
      "ddGKIN_H2O": -11.55,
      "mf": -6.28,
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      "PhiF_H2O": -0.11,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb755",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A89L,F103L",
      "MUTATION_PDB": "A89L,F103L",
      "SEC_STR": "Beta,Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.95,
      "dln(kf)_H2O": 0.54,
      "ln(ku)_H2O": 4.52,
      "dln(ku)_H2O": 5.19,
      "ddGKIN_H2O": -11.55,
      "mf": -6.28,
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      "PhiF_H2O": -0.11,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb755",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L101V",
      "MUTATION_PDB": "L101V",
      "SEC_STR": "Coil",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.23,
      "dln(kf)_H2O": -0.18,
      "ln(ku)_H2O": 1.9,
      "dln(ku)_H2O": 2.57,
      "ddGKIN_H2O": -6.82,
      "mf": -8.95,
      "mu": 3.89,
      "PhiF_H2O": 0.06,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb756",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L101V",
      "MUTATION_PDB": "L101V",
      "SEC_STR": "Coil",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.23,
      "dln(kf)_H2O": -0.18,
      "ln(ku)_H2O": 1.9,
      "dln(ku)_H2O": 2.57,
      "ddGKIN_H2O": -6.82,
      "mf": -8.95,
      "mu": 3.89,
      "PhiF_H2O": 0.06,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb756",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L101I",
      "MUTATION_PDB": "L101I",
      "SEC_STR": "Coil",
      "RSA": "4.9",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.49,
      "dln(kf)_H2O": 0.08,
      "ln(ku)_H2O": 0.59,
      "dln(ku)_H2O": 1.26,
      "ddGKIN_H2O": -2.89,
      "mf": -8.66,
      "mu": 4.14,
      "PhiF_H2O": -0.07,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb757",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L101I",
      "MUTATION_PDB": "L101I",
      "SEC_STR": "Coil",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.49,
      "dln(kf)_H2O": 0.08,
      "ln(ku)_H2O": 0.59,
      "dln(ku)_H2O": 1.26,
      "ddGKIN_H2O": -2.89,
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      "PhiF_H2O": -0.07,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb757",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L101F",
      "MUTATION_PDB": "L101F",
      "SEC_STR": "Coil",
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      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(kf)_H2O": 0.31,
      "ln(ku)_H2O": 1.67,
      "dln(ku)_H2O": 2.34,
      "ddGKIN_H2O": -5.02,
      "mf": -8.62,
      "mu": 4.14,
      "PhiF_H2O": -0.15,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb758",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "L101F",
      "MUTATION_PDB": "L101F",
      "SEC_STR": "Coil",
      "RSA": "4.9",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.72,
      "dln(kf)_H2O": 0.31,
      "ln(ku)_H2O": 1.67,
      "dln(ku)_H2O": 2.34,
      "ddGKIN_H2O": -5.02,
      "mf": -8.62,
      "mu": 4.14,
      "PhiF_H2O": -0.15,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb758",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103S",
      "MUTATION_PDB": "F103S",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.73,
      "dln(kf)_H2O": -0.68,
      "ln(ku)_H2O": 3.77,
      "dln(ku)_H2O": 4.44,
      "ddGKIN_H2O": -12.68,
      "mf": -6.95,
      "mu": 2.01,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb759",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103S",
      "MUTATION_PDB": "F103S",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.73,
      "dln(kf)_H2O": -0.68,
      "ln(ku)_H2O": 3.77,
      "dln(ku)_H2O": 4.44,
      "ddGKIN_H2O": -12.68,
      "mf": -6.95,
      "mu": 2.01,
      "PhiF_H2O": 0.13,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb759",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103A",
      "MUTATION_PDB": "F103A",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.49,
      "dln(kf)_H2O": -0.92,
      "ln(ku)_H2O": 2.49,
      "dln(ku)_H2O": 3.16,
      "ddGKIN_H2O": -10.08,
      "mf": -7.24,
      "mu": 2.93,
      "PhiF_H2O": 0.22,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb760",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103A",
      "MUTATION_PDB": "F103A",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.49,
      "dln(kf)_H2O": -0.92,
      "ln(ku)_H2O": 2.49,
      "dln(ku)_H2O": 3.16,
      "ddGKIN_H2O": -10.08,
      "mf": -7.24,
      "mu": 2.93,
      "PhiF_H2O": 0.22,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb760",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103V",
      "MUTATION_PDB": "F103V",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.49,
      "dln(kf)_H2O": 0.08,
      "ln(ku)_H2O": 2.58,
      "dln(ku)_H2O": 3.25,
      "ddGKIN_H2O": -7.87,
      "mf": -7.74,
      "mu": 4.39,
      "PhiF_H2O": -0.03,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb761",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103V",
      "MUTATION_PDB": "F103V",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.49,
      "dln(kf)_H2O": 0.08,
      "ln(ku)_H2O": 2.58,
      "dln(ku)_H2O": 3.25,
      "ddGKIN_H2O": -7.87,
      "mf": -7.74,
      "mu": 4.39,
      "PhiF_H2O": -0.03,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb761",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103L",
      "MUTATION_PDB": "F103L",
      "SEC_STR": "Beta",
      "RSA": "2.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.43,
      "dln(kf)_H2O": 0.02,
      "ln(ku)_H2O": 1.22,
      "dln(ku)_H2O": 1.89,
      "ddGKIN_H2O": -4.64,
      "mf": -7.41,
      "mu": 3.56,
      "PhiF_H2O": -0.01,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb762",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F103L",
      "MUTATION_PDB": "F103L",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.43,
      "dln(kf)_H2O": 0.02,
      "ln(ku)_H2O": 1.22,
      "dln(ku)_H2O": 1.89,
      "ddGKIN_H2O": -4.64,
      "mf": -7.41,
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      "PhiF_H2O": -0.01,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb762",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F109V",
      "MUTATION_PDB": "F109V",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.86,
      "dln(kf)_H2O": -0.55,
      "ln(ku)_H2O": 2.33,
      "dln(ku)_H2O": 3.0,
      "ddGKIN_H2O": -8.83,
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      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb763",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F109V",
      "MUTATION_PDB": "F109V",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.86,
      "dln(kf)_H2O": -0.55,
      "ln(ku)_H2O": 2.33,
      "dln(ku)_H2O": 3.0,
      "ddGKIN_H2O": -8.83,
      "mf": -6.57,
      "mu": 4.18,
      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb763",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F109I",
      "MUTATION_PDB": "F109I",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.48,
      "dln(kf)_H2O": 0.07,
      "ln(ku)_H2O": 2.77,
      "dln(ku)_H2O": 3.44,
      "ddGKIN_H2O": -8.33,
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      "PhiF_H2O": -0.02,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb764",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F109I",
      "MUTATION_PDB": "F109I",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.48,
      "dln(kf)_H2O": 0.07,
      "ln(ku)_H2O": 2.77,
      "dln(ku)_H2O": 3.44,
      "ddGKIN_H2O": -8.33,
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      "PhiF_H2O": -0.02,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb764",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F109L",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.64,
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      "dln(ku)_H2O": 1.5,
      "ddGKIN_H2O": -3.18,
      "mf": -7.91,
      "mu": 3.89,
      "PhiF_H2O": -0.18,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb765",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "F109L",
      "MUTATION_PDB": "F109L",
      "SEC_STR": "Beta",
      "RSA": "0.0",
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      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.64,
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      "dln(ku)_H2O": 1.5,
      "ddGKIN_H2O": -3.18,
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      "PhiF_H2O": -0.18,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb765",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111S",
      "MUTATION_PDB": "I111S",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb766",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111S",
      "MUTATION_PDB": "I111S",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "ln(ku)_H2O": 0.88,
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      "ddGKIN_H2O": -12.72,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb766",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111A",
      "MUTATION_PDB": "I111A",
      "SEC_STR": "Beta",
      "RSA": "17.8",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 0.22,
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      "dln(ku)_H2O": 1.26,
      "ddGKIN_H2O": -11.05,
      "mf": -7.95,
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      "PhiF_H2O": 0.71,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb767",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111A",
      "MUTATION_PDB": "I111A",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 0.22,
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      "dln(ku)_H2O": 1.26,
      "ddGKIN_H2O": -11.05,
      "mf": -7.95,
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      "PhiF_H2O": 0.71,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb767",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111V",
      "MUTATION_PDB": "I111V",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb768",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111V",
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      "SEC_STR": "Beta",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(ku)_H2O": -0.15,
      "ddGKIN_H2O": -0.67,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb768",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111L",
      "MUTATION_PDB": "I111L",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(ku)_H2O": 1.26,
      "ddGKIN_H2O": -4.23,
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      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb769",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111L",
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      "BUFFER_NAME": "Tris",
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      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(ku)_H2O": 1.26,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb769",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111F",
      "MUTATION_PDB": "I111F",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb770",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I111F",
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      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
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      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "ddGKIN_H2O": -11.34,
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      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb770",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122S",
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      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb771",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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         "1shfA00 (2.30.30.40)"
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      "MEASURE_KIN": "stopped-flow",
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      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb771",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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         "1shfA00 (2.30.30.40)"
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      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.46,
      "dln(kf)_H2O": -1.95,
      "ln(ku)_H2O": -0.36,
      "dln(ku)_H2O": 0.31,
      "ddGKIN_H2O": -5.65,
      "mf": -8.95,
      "mu": 3.56,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb772",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G",
      "MUTATION_PDB": "A122G",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.46,
      "dln(kf)_H2O": -1.95,
      "ln(ku)_H2O": -0.36,
      "dln(ku)_H2O": 0.31,
      "ddGKIN_H2O": -5.65,
      "mf": -8.95,
      "mu": 3.56,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb772",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V",
      "MUTATION_PDB": "A122V",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.49,
      "dln(kf)_H2O": 2.08,
      "ln(ku)_H2O": 1.1,
      "dln(ku)_H2O": 1.77,
      "ddGKIN_H2O": 0.75,
      "mf": -8.41,
      "mu": 4.56,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb773",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V",
      "MUTATION_PDB": "A122V",
      "SEC_STR": "Beta",
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      "T": 25.0,
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.49,
      "dln(kf)_H2O": 2.08,
      "ln(ku)_H2O": 1.1,
      "dln(ku)_H2O": 1.77,
      "ddGKIN_H2O": 0.75,
      "mf": -8.41,
      "mu": 4.56,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb773",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122L",
      "MUTATION_PDB": "A122L",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.87,
      "dln(kf)_H2O": -1.54,
      "ln(ku)_H2O": 1.84,
      "dln(ku)_H2O": 2.51,
      "ddGKIN_H2O": -10.0,
      "mf": -8.66,
      "mu": 3.56,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb774",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122L",
      "MUTATION_PDB": "A122L",
      "SEC_STR": "Beta",
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      "T": 25.0,
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.87,
      "dln(kf)_H2O": -1.54,
      "ln(ku)_H2O": 1.84,
      "dln(ku)_H2O": 2.51,
      "ddGKIN_H2O": -10.0,
      "mf": -8.66,
      "mu": 3.56,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb774",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122F",
      "MUTATION_PDB": "A122F",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.63,
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      "ln(ku)_H2O": 3.27,
      "dln(ku)_H2O": 3.94,
      "ddGKIN_H2O": -9.2,
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      "PhiF_H2O": -0.06,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb775",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122F",
      "MUTATION_PDB": "A122F",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.63,
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      "ln(ku)_H2O": 3.27,
      "dln(ku)_H2O": 3.94,
      "ddGKIN_H2O": -9.2,
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      "PhiF_H2O": -0.06,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb775",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133A",
      "MUTATION_PDB": "I133A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
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      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.44,
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      "dln(ku)_H2O": 3.29,
      "ddGKIN_H2O": -13.05,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb776",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133A",
      "MUTATION_PDB": "I133A",
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      "BUFFER_NAME": "Tris",
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      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.44,
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      "ln(ku)_H2O": 2.62,
      "dln(ku)_H2O": 3.29,
      "ddGKIN_H2O": -13.05,
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      "PhiF_H2O": 0.37,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb776",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133V",
      "MUTATION_PDB": "I133V",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(ku)_H2O": -0.2,
      "ddGKIN_H2O": -0.17,
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      "mu": 2.76,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb777",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133V",
      "MUTATION_PDB": "I133V",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.17,
      "dln(kf)_H2O": -0.24,
      "ln(ku)_H2O": -0.87,
      "dln(ku)_H2O": -0.2,
      "ddGKIN_H2O": -0.17,
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      "mu": 2.76,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb777",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133L",
      "MUTATION_PDB": "I133L",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.87,
      "dln(kf)_H2O": -0.54,
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      "dln(ku)_H2O": 0.77,
      "ddGKIN_H2O": -3.14,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb778",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133L",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.87,
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      "dln(ku)_H2O": 0.77,
      "ddGKIN_H2O": -3.14,
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      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb778",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133F",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.28,
      "dln(kf)_H2O": -0.13,
      "ln(ku)_H2O": 5.08,
      "dln(ku)_H2O": 5.75,
      "ddGKIN_H2O": -14.52,
      "mf": -7.45,
      "mu": 3.39,
      "PhiF_H2O": 0.02,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb779",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "I133F",
      "MUTATION_PDB": "I133F",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.28,
      "dln(kf)_H2O": -0.13,
      "ln(ku)_H2O": 5.08,
      "dln(ku)_H2O": 5.75,
      "ddGKIN_H2O": -14.52,
      "mf": -7.45,
      "mu": 3.39,
      "PhiF_H2O": 0.02,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb779",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138A",
      "MUTATION_PDB": "V138A",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.37,
      "dln(kf)_H2O": -0.04,
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      "dln(ku)_H2O": 3.56,
      "ddGKIN_H2O": -8.91,
      "mf": -8.16,
      "mu": 4.02,
      "PhiF_H2O": 0.01,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb780",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138A",
      "MUTATION_PDB": "V138A",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.37,
      "dln(kf)_H2O": -0.04,
      "ln(ku)_H2O": 2.89,
      "dln(ku)_H2O": 3.56,
      "ddGKIN_H2O": -8.91,
      "mf": -8.16,
      "mu": 4.02,
      "PhiF_H2O": 0.01,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb780",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138I",
      "MUTATION_PDB": "V138I",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.96,
      "dln(kf)_H2O": 0.55,
      "ln(ku)_H2O": -0.42,
      "dln(ku)_H2O": 0.25,
      "ddGKIN_H2O": 0.71,
      "mf": -9.08,
      "mu": 4.14,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb781",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138I",
      "MUTATION_PDB": "V138I",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.96,
      "dln(kf)_H2O": 0.55,
      "ln(ku)_H2O": -0.42,
      "dln(ku)_H2O": 0.25,
      "ddGKIN_H2O": 0.71,
      "mf": -9.08,
      "mu": 4.14,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb781",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138L",
      "MUTATION_PDB": "V138L",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.99,
      "dln(kf)_H2O": 0.58,
      "ln(ku)_H2O": 0.11,
      "dln(ku)_H2O": 0.78,
      "ddGKIN_H2O": -0.5,
      "mf": -8.7,
      "mu": 4.31,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb782",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138L",
      "MUTATION_PDB": "V138L",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.99,
      "dln(kf)_H2O": 0.58,
      "ln(ku)_H2O": 0.11,
      "dln(ku)_H2O": 0.78,
      "ddGKIN_H2O": -0.5,
      "mf": -8.7,
      "mu": 4.31,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb782",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138F",
      "MUTATION_PDB": "V138F",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.43,
      "dln(kf)_H2O": 1.02,
      "ln(ku)_H2O": 1.59,
      "dln(ku)_H2O": 2.26,
      "ddGKIN_H2O": -3.05,
      "mf": -8.45,
      "mu": 4.27,
      "PhiF_H2O": -0.82,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb783",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138F",
      "MUTATION_PDB": "V138F",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.43,
      "dln(kf)_H2O": 1.02,
      "ln(ku)_H2O": 1.59,
      "dln(ku)_H2O": 2.26,
      "ddGKIN_H2O": -3.05,
      "mf": -8.45,
      "mu": 4.27,
      "PhiF_H2O": -0.82,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb783",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G,V138I",
      "MUTATION_PDB": "A122G,V138I",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.63,
      "dln(kf)_H2O": -1.78,
      "ln(ku)_H2O": -0.4,
      "dln(ku)_H2O": 0.27,
      "ddGKIN_H2O": -5.06,
      "mf": -8.95,
      "mu": 3.43,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb784",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G,V138I",
      "MUTATION_PDB": "A122G,V138I",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
      "T": 25.0,
      "pH": 8.0,
      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.63,
      "dln(kf)_H2O": -1.78,
      "ln(ku)_H2O": -0.4,
      "dln(ku)_H2O": 0.27,
      "ddGKIN_H2O": -5.06,
      "mf": -8.95,
      "mu": 3.43,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb784",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V,V138I",
      "MUTATION_PDB": "A122V,V138I",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
      "T": 25.0,
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.06,
      "dln(kf)_H2O": 2.65,
      "ln(ku)_H2O": 0.99,
      "dln(ku)_H2O": 1.66,
      "ddGKIN_H2O": 2.26,
      "mf": -8.49,
      "mu": 4.77,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb785",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V,V138I",
      "MUTATION_PDB": "A122V,V138I",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.06,
      "dln(kf)_H2O": 2.65,
      "ln(ku)_H2O": 0.99,
      "dln(ku)_H2O": 1.66,
      "ddGKIN_H2O": 2.26,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb785",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G,V138L",
      "MUTATION_PDB": "A122G,V138L",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 1.72,
      "dln(kf)_H2O": -1.69,
      "ln(ku)_H2O": -0.78,
      "dln(ku)_H2O": -0.11,
      "ddGKIN_H2O": -3.93,
      "mf": -9.12,
      "mu": 3.1,
      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb786",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G,V138L",
      "MUTATION_PDB": "A122G,V138L",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
      "T": 25.0,
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(ku)_H2O": -0.11,
      "ddGKIN_H2O": -3.93,
      "mf": -9.12,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb786",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V,V138L",
      "MUTATION_PDB": "A122V,V138L",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "mf": -8.12,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb787",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V,V138L",
      "MUTATION_PDB": "A122V,V138L",
      "SEC_STR": "Beta,Beta",
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      "BUFFER_CONC": "0.01",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb787",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G,V138F",
      "MUTATION_PDB": "A122G,V138F",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
      "T": 25.0,
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.37,
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      "dln(ku)_H2O": 1.24,
      "ddGKIN_H2O": -5.65,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb788",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122G,V138F",
      "MUTATION_PDB": "A122G,V138F",
      "SEC_STR": "Beta,Beta",
      "RSA": "0.0,9.2",
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      "BUFFER_NAME": "Tris",
      "BUFFER_CONC": "0.01",
      "ADDITIVES": "0.2 mM EDTA",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "ddGKIN_H2O": -5.65,
      "mf": -10.25,
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      "AUTHOR_KIN": "Northey, J.G.B., Di Nardo, A.A., Davidson, A.R.",
      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb788",
      "YEAR_KIN": 2002.0,
      "PMID_KIN": "11786916",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V,V138F",
      "MUTATION_PDB": "A122V,V138F",
      "SEC_STR": "Beta,Beta",
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      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb789",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
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         "PF00018"
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      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "A122V,V138F",
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      "MEASURE_KIN": "stopped-flow",
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      "ddGKIN_H2O": -5.69,
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      "REFERENCE_KIN": "Hydrophobic core packing in the SH3 domain folding transition state. Nat. Struct. Biol. 9, 126\u2013130. https://doi.org/10.1038/nsb789",
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      "PMID_KIN": "11786916",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
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      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
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      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.01",
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      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR,  Chan HS",
      "REFERENCE_KIN": "Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999\u201310004. https://doi.org/10.1073/pnas.0801874105",
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      "PMID_KIN": "18626019",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
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      "MUTATED_CHAIN": "A",
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         "1shfA00 (2.30.30.40)"
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      "REFERENCE_KIN": "Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A 105(29): 9999\u201310004. https://doi.org/10.1073/pnas.0801874105",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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   {
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      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.01",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.2,
      "mu": 2.4,
      "beta-T": 0.68,
      "AUTHOR_KIN": "Lin SL, Zarrine-Afsar A, Davidson AR",
      "REFERENCE_KIN": "The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19241379",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "N136V",
      "MUTATION_PDB": "N136V",
      "SEC_STR": "Helix",
      "RSA": "78.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.01",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.2,
      "mu": 2.4,
      "beta-T": 0.68,
      "AUTHOR_KIN": "Lin SL, Zarrine-Afsar A, Davidson AR",
      "REFERENCE_KIN": "The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19241379",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138L",
      "MUTATION_PDB": "V138L",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.01",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.03,
      "mu": 2.43,
      "beta-T": 0.67,
      "AUTHOR_KIN": "Lin SL, Zarrine-Afsar A, Davidson AR",
      "REFERENCE_KIN": "The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19241379",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "Fyn SH3",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "P06241",
      "PDB_wild": "1shf",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shfA00 (2.30.30.40)"
      ],
      "EC_NUMBER": "2.7.10.2",
      "MUTATION_UNIPROT": "V138L",
      "MUTATION_PDB": "V138L",
      "SEC_STR": "Beta",
      "RSA": "9.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.01",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -5.03,
      "mu": 2.43,
      "beta-T": 0.67,
      "AUTHOR_KIN": "Lin SL, Zarrine-Afsar A, Davidson AR",
      "REFERENCE_KIN": "The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Sci 18(3):526-36. https://doi.org/10.1002/pro.52",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19241379",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.4,
      "dln(kf)_H2O": 5.4,
      "ln(ku)_H2O": -9.16,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9384",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.4,
      "dln(kf)_H2O": 5.4,
      "ln(ku)_H2O": -9.16,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9384",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "F6A",
      "MUTATION_PDB": "F5A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.15,
      "dln(kf)_H2O": -1.25,
      "ln(ku)_H2O": -5.68,
      "dln(ku)_H2O": 3.48,
      "ddGKIN_H2O": -10.93,
      "PhiF_H2O": 0.74,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9385",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "F6A",
      "MUTATION_PDB": "F5A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.15,
      "dln(kf)_H2O": -1.25,
      "ln(ku)_H2O": -5.68,
      "dln(ku)_H2O": 3.48,
      "ddGKIN_H2O": -10.93,
      "PhiF_H2O": 0.74,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9385",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "A10G",
      "MUTATION_PDB": "A9G",
      "SEC_STR": "Helix",
      "RSA": "6.6",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -6.76,
      "dln(ku)_H2O": 2.4,
      "ddGKIN_H2O": -8.32,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9386",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "A10G",
      "MUTATION_PDB": "A9G",
      "SEC_STR": "Helix",
      "RSA": "6.6",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -6.76,
      "dln(ku)_H2O": 2.4,
      "ddGKIN_H2O": -8.32,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9386",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "V13A",
      "MUTATION_PDB": "V12A",
      "SEC_STR": "Helix",
      "RSA": "7.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.29,
      "dln(kf)_H2O": -1.11,
      "ln(ku)_H2O": -7.58,
      "dln(ku)_H2O": 1.58,
      "ddGKIN_H2O": -6.21,
      "PhiF_H2O": 0.59,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9387",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "V13A",
      "MUTATION_PDB": "V12A",
      "SEC_STR": "Helix",
      "RSA": "7.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.29,
      "dln(kf)_H2O": -1.11,
      "ln(ku)_H2O": -7.58,
      "dln(ku)_H2O": 1.58,
      "ddGKIN_H2O": -6.21,
      "PhiF_H2O": 0.59,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9387",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L16A",
      "MUTATION_PDB": "L15A",
      "SEC_STR": "Coil",
      "RSA": "0.6",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.24,
      "dln(kf)_H2O": -2.16,
      "ln(ku)_H2O": -4.89,
      "dln(ku)_H2O": 4.27,
      "ddGKIN_H2O": -14.86,
      "PhiF_H2O": 0.66,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9388",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L16A",
      "MUTATION_PDB": "L15A",
      "SEC_STR": "Coil",
      "RSA": "0.6",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.24,
      "dln(kf)_H2O": -2.16,
      "ln(ku)_H2O": -4.89,
      "dln(ku)_H2O": 4.27,
      "ddGKIN_H2O": -14.86,
      "PhiF_H2O": 0.66,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9388",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "P20A",
      "MUTATION_PDB": "P19A",
      "SEC_STR": "Coil",
      "RSA": "5.9",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.76,
      "dln(kf)_H2O": 0.36,
      "ln(ku)_H2O": -7.17,
      "dln(ku)_H2O": 1.99,
      "ddGKIN_H2O": -3.76,
      "PhiF_H2O": 1.22,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9389",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "P20A",
      "MUTATION_PDB": "P19A",
      "SEC_STR": "Coil",
      "RSA": "5.9",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.76,
      "dln(kf)_H2O": 0.36,
      "ln(ku)_H2O": -7.17,
      "dln(ku)_H2O": 1.99,
      "ddGKIN_H2O": -3.76,
      "PhiF_H2O": 1.22,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9389",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "D22A",
      "MUTATION_PDB": "D21A",
      "SEC_STR": "Helix",
      "RSA": "20.2",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.76,
      "dln(kf)_H2O": 0.36,
      "ln(ku)_H2O": -8.09,
      "dln(ku)_H2O": 1.07,
      "ddGKIN_H2O": -1.64,
      "PhiF_H2O": 1.49,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9390",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "D22A",
      "MUTATION_PDB": "D21A",
      "SEC_STR": "Helix",
      "RSA": "20.2",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.76,
      "dln(kf)_H2O": 0.36,
      "ln(ku)_H2O": -8.09,
      "dln(ku)_H2O": 1.07,
      "ddGKIN_H2O": -1.64,
      "PhiF_H2O": 1.49,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9390",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L26A",
      "MUTATION_PDB": "L25A",
      "SEC_STR": "Helix",
      "RSA": "9.8",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.59,
      "dln(kf)_H2O": 0.19,
      "ln(ku)_H2O": -5.33,
      "dln(ku)_H2O": 3.83,
      "ddGKIN_H2O": -8.41,
      "PhiF_H2O": 1.05,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9391",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L26A",
      "MUTATION_PDB": "L25A",
      "SEC_STR": "Helix",
      "RSA": "9.8",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.59,
      "dln(kf)_H2O": 0.19,
      "ln(ku)_H2O": -5.33,
      "dln(ku)_H2O": 3.83,
      "ddGKIN_H2O": -8.41,
      "PhiF_H2O": 1.05,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9391",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "F27A",
      "MUTATION_PDB": "F26A",
      "SEC_STR": "Helix",
      "RSA": "25.9",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.34,
      "dln(kf)_H2O": -0.06,
      "ln(ku)_H2O": -6.27,
      "dln(ku)_H2O": 2.89,
      "ddGKIN_H2O": -6.82,
      "PhiF_H2O": 0.98,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9392",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "F27A",
      "MUTATION_PDB": "F26A",
      "SEC_STR": "Helix",
      "RSA": "25.9",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.34,
      "dln(kf)_H2O": -0.06,
      "ln(ku)_H2O": -6.27,
      "dln(ku)_H2O": 2.89,
      "ddGKIN_H2O": -6.82,
      "PhiF_H2O": 0.98,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9392",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y29A",
      "MUTATION_PDB": "Y28A",
      "SEC_STR": "Helix",
      "RSA": "27.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.64,
      "dln(kf)_H2O": 1.24,
      "ln(ku)_H2O": -3.38,
      "dln(ku)_H2O": 5.78,
      "ddGKIN_H2O": -10.49,
      "PhiF_H2O": 1.27,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9393",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y29A",
      "MUTATION_PDB": "Y28A",
      "SEC_STR": "Helix",
      "RSA": "27.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.64,
      "dln(kf)_H2O": 1.24,
      "ln(ku)_H2O": -3.38,
      "dln(ku)_H2O": 5.78,
      "ddGKIN_H2O": -10.49,
      "PhiF_H2O": 1.27,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9393",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y29N",
      "MUTATION_PDB": "Y28N",
      "SEC_STR": "Helix",
      "RSA": "27.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.9,
      "dln(kf)_H2O": 0.5,
      "ln(ku)_H2O": -4.23,
      "dln(ku)_H2O": 4.93,
      "ddGKIN_H2O": -10.24,
      "PhiF_H2O": 1.11,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9394",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y29N",
      "MUTATION_PDB": "Y28N",
      "SEC_STR": "Helix",
      "RSA": "27.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.9,
      "dln(kf)_H2O": 0.5,
      "ln(ku)_H2O": -4.23,
      "dln(ku)_H2O": 4.93,
      "ddGKIN_H2O": -10.24,
      "PhiF_H2O": 1.11,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9394",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y29F",
      "MUTATION_PDB": "Y28F",
      "SEC_STR": "Helix",
      "RSA": "27.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.93,
      "dln(kf)_H2O": 0.53,
      "ln(ku)_H2O": -6.36,
      "dln(ku)_H2O": 2.8,
      "ddGKIN_H2O": -5.24,
      "PhiF_H2O": 1.23,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9395",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y29F",
      "MUTATION_PDB": "Y28F",
      "SEC_STR": "Helix",
      "RSA": "27.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.93,
      "dln(kf)_H2O": 0.53,
      "ln(ku)_H2O": -6.36,
      "dln(ku)_H2O": 2.8,
      "ddGKIN_H2O": -5.24,
      "PhiF_H2O": 1.23,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9395",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y32N",
      "MUTATION_PDB": "Y31N",
      "SEC_STR": "Helix",
      "RSA": "28.8",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.42,
      "dln(kf)_H2O": 0.02,
      "ln(ku)_H2O": -7.39,
      "dln(ku)_H2O": 1.77,
      "ddGKIN_H2O": -4.04,
      "PhiF_H2O": 1.01,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9396",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y32N",
      "MUTATION_PDB": "Y31N",
      "SEC_STR": "Helix",
      "RSA": "28.8",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.42,
      "dln(kf)_H2O": 0.02,
      "ln(ku)_H2O": -7.39,
      "dln(ku)_H2O": 1.77,
      "ddGKIN_H2O": -4.04,
      "PhiF_H2O": 1.01,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9396",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K33A",
      "MUTATION_PDB": "K32A",
      "SEC_STR": "Helix",
      "RSA": "28.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.24,
      "dln(kf)_H2O": 0.84,
      "ln(ku)_H2O": -5.44,
      "dln(ku)_H2O": 3.72,
      "ddGKIN_H2O": -6.65,
      "PhiF_H2O": 1.29,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9397",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K33A",
      "MUTATION_PDB": "K32A",
      "SEC_STR": "Helix",
      "RSA": "28.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.24,
      "dln(kf)_H2O": 0.84,
      "ln(ku)_H2O": -5.44,
      "dln(ku)_H2O": 3.72,
      "ddGKIN_H2O": -6.65,
      "PhiF_H2O": 1.29,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9397",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K33E",
      "MUTATION_PDB": "K32E",
      "SEC_STR": "Helix",
      "RSA": "28.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.29,
      "dln(kf)_H2O": -0.11,
      "ln(ku)_H2O": -6.63,
      "dln(ku)_H2O": 2.53,
      "ddGKIN_H2O": -6.1,
      "PhiF_H2O": 0.96,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9398",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K33E",
      "MUTATION_PDB": "K32E",
      "SEC_STR": "Helix",
      "RSA": "28.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.29,
      "dln(kf)_H2O": -0.11,
      "ln(ku)_H2O": -6.63,
      "dln(ku)_H2O": 2.53,
      "ddGKIN_H2O": -6.1,
      "PhiF_H2O": 0.96,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9398",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K33R",
      "MUTATION_PDB": "K32R",
      "SEC_STR": "Helix",
      "RSA": "28.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.85,
      "dln(kf)_H2O": -0.55,
      "ln(ku)_H2O": -5.72,
      "dln(ku)_H2O": 3.44,
      "ddGKIN_H2O": -9.22,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9399",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K33R",
      "MUTATION_PDB": "K32R",
      "SEC_STR": "Helix",
      "RSA": "28.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.85,
      "dln(kf)_H2O": -0.55,
      "ln(ku)_H2O": -5.72,
      "dln(ku)_H2O": 3.44,
      "ddGKIN_H2O": -9.22,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9399",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Q34A",
      "MUTATION_PDB": "Q33A",
      "SEC_STR": "Helix",
      "RSA": "1.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.44,
      "dln(kf)_H2O": 2.04,
      "ln(ku)_H2O": -1.67,
      "dln(ku)_H2O": 7.49,
      "ddGKIN_H2O": -12.59,
      "PhiF_H2O": 1.37,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9400",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Q34A",
      "MUTATION_PDB": "Q33A",
      "SEC_STR": "Helix",
      "RSA": "1.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.44,
      "dln(kf)_H2O": 2.04,
      "ln(ku)_H2O": -1.67,
      "dln(ku)_H2O": 7.49,
      "ddGKIN_H2O": -12.59,
      "PhiF_H2O": 1.37,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9400",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "A35G",
      "MUTATION_PDB": "A34G",
      "SEC_STR": "Helix",
      "RSA": "8.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.78,
      "dln(kf)_H2O": 0.38,
      "ln(ku)_H2O": -6.84,
      "dln(ku)_H2O": 2.32,
      "ddGKIN_H2O": -4.48,
      "PhiF_H2O": 1.19,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9401",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "A35G",
      "MUTATION_PDB": "A34G",
      "SEC_STR": "Helix",
      "RSA": "8.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.78,
      "dln(kf)_H2O": 0.38,
      "ln(ku)_H2O": -6.84,
      "dln(ku)_H2O": 2.32,
      "ddGKIN_H2O": -4.48,
      "PhiF_H2O": 1.19,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9401",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "T36A",
      "MUTATION_PDB": "T35A",
      "SEC_STR": "Helix",
      "RSA": "34.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.23,
      "dln(kf)_H2O": 0.83,
      "ln(ku)_H2O": -6.03,
      "dln(ku)_H2O": 3.13,
      "ddGKIN_H2O": -5.31,
      "PhiF_H2O": 1.36,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9402",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "T36A",
      "MUTATION_PDB": "T35A",
      "SEC_STR": "Helix",
      "RSA": "34.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.23,
      "dln(kf)_H2O": 0.83,
      "ln(ku)_H2O": -6.03,
      "dln(ku)_H2O": 3.13,
      "ddGKIN_H2O": -5.31,
      "PhiF_H2O": 1.36,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9402",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "I40A",
      "MUTATION_PDB": "I39A",
      "SEC_STR": "Coil",
      "RSA": "4.1",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.51,
      "dln(kf)_H2O": 0.11,
      "ln(ku)_H2O": -7.15,
      "dln(ku)_H2O": 2.01,
      "ddGKIN_H2O": -4.39,
      "PhiF_H2O": 1.05,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9403",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "I40A",
      "MUTATION_PDB": "I39A",
      "SEC_STR": "Coil",
      "RSA": "4.1",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.51,
      "dln(kf)_H2O": 0.11,
      "ln(ku)_H2O": -7.15,
      "dln(ku)_H2O": 2.01,
      "ddGKIN_H2O": -4.39,
      "PhiF_H2O": 1.05,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9403",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "P45A",
      "MUTATION_PDB": "P44A",
      "SEC_STR": "Coil",
      "RSA": "35.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.38,
      "dln(kf)_H2O": -0.02,
      "ln(ku)_H2O": -6.98,
      "dln(ku)_H2O": 2.18,
      "ddGKIN_H2O": -5.08,
      "PhiF_H2O": 0.99,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9404",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "P45A",
      "MUTATION_PDB": "P44A",
      "SEC_STR": "Coil",
      "RSA": "35.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.38,
      "dln(kf)_H2O": -0.02,
      "ln(ku)_H2O": -6.98,
      "dln(ku)_H2O": 2.18,
      "ddGKIN_H2O": -5.08,
      "PhiF_H2O": 0.99,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9404",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K53M",
      "MUTATION_PDB": "K52M",
      "SEC_STR": "Helix",
      "RSA": "35.1",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.93,
      "dln(kf)_H2O": 0.53,
      "ln(ku)_H2O": -9.5,
      "dln(ku)_H2O": -0.34,
      "ddGKIN_H2O": 2.01,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9405",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K53M",
      "MUTATION_PDB": "K52M",
      "SEC_STR": "Helix",
      "RSA": "35.1",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.93,
      "dln(kf)_H2O": 0.53,
      "ln(ku)_H2O": -9.5,
      "dln(ku)_H2O": -0.34,
      "ddGKIN_H2O": 2.01,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9405",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K55A",
      "MUTATION_PDB": "K54A",
      "SEC_STR": "Helix",
      "RSA": "22.4",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.93,
      "dln(kf)_H2O": -0.47,
      "ln(ku)_H2O": -7.1,
      "dln(ku)_H2O": 2.06,
      "ddGKIN_H2O": -5.85,
      "PhiF_H2O": 0.81,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9406",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K55A",
      "MUTATION_PDB": "K54A",
      "SEC_STR": "Helix",
      "RSA": "22.4",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.93,
      "dln(kf)_H2O": -0.47,
      "ln(ku)_H2O": -7.1,
      "dln(ku)_H2O": 2.06,
      "ddGKIN_H2O": -5.85,
      "PhiF_H2O": 0.81,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9406",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K55M",
      "MUTATION_PDB": "K54M",
      "SEC_STR": "Helix",
      "RSA": "22.4",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.07,
      "dln(kf)_H2O": -0.33,
      "ln(ku)_H2O": -9.11,
      "dln(ku)_H2O": 0.05,
      "ddGKIN_H2O": -0.88,
      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9407",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "K55M",
      "MUTATION_PDB": "K54M",
      "SEC_STR": "Helix",
      "RSA": "22.4",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.07,
      "dln(kf)_H2O": -0.33,
      "ln(ku)_H2O": -9.11,
      "dln(ku)_H2O": 0.05,
      "ddGKIN_H2O": -0.88,
      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9407",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "E68A",
      "MUTATION_PDB": "E67A",
      "SEC_STR": "Helix",
      "RSA": "56.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.34,
      "dln(kf)_H2O": 0.94,
      "ln(ku)_H2O": -6.79,
      "dln(ku)_H2O": 2.37,
      "ddGKIN_H2O": -3.3,
      "PhiF_H2O": 1.65,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9408",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "E68A",
      "MUTATION_PDB": "E67A",
      "SEC_STR": "Helix",
      "RSA": "56.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.34,
      "dln(kf)_H2O": 0.94,
      "ln(ku)_H2O": -6.79,
      "dln(ku)_H2O": 2.37,
      "ddGKIN_H2O": -3.3,
      "PhiF_H2O": 1.65,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9408",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "A70G",
      "MUTATION_PDB": "A69G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.3,
      "dln(kf)_H2O": -0.1,
      "ln(ku)_H2O": -6.3,
      "dln(ku)_H2O": 2.86,
      "ddGKIN_H2O": -6.84,
      "PhiF_H2O": 0.96,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9409",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "A70G",
      "MUTATION_PDB": "A69G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.3,
      "dln(kf)_H2O": -0.1,
      "ln(ku)_H2O": -6.3,
      "dln(ku)_H2O": 2.86,
      "ddGKIN_H2O": -6.84,
      "PhiF_H2O": 0.96,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9409",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y74A",
      "MUTATION_PDB": "Y73A",
      "SEC_STR": "Helix",
      "RSA": "3.2",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.97,
      "dln(kf)_H2O": -2.43,
      "ln(ku)_H2O": -3.47,
      "dln(ku)_H2O": 5.69,
      "ddGKIN_H2O": -18.77,
      "PhiF_H2O": 0.7,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9410",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y74A",
      "MUTATION_PDB": "Y73A",
      "SEC_STR": "Helix",
      "RSA": "3.2",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.97,
      "dln(kf)_H2O": -2.43,
      "ln(ku)_H2O": -3.47,
      "dln(ku)_H2O": 5.69,
      "ddGKIN_H2O": -18.77,
      "PhiF_H2O": 0.7,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9410",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y74F",
      "MUTATION_PDB": "Y73F",
      "SEC_STR": "Helix",
      "RSA": "3.2",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.11,
      "dln(kf)_H2O": 0.71,
      "ln(ku)_H2O": -8.52,
      "dln(ku)_H2O": 0.64,
      "ddGKIN_H2O": 0.16,
      "PhiF_H2O": -10.9,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9411",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y74F",
      "MUTATION_PDB": "Y73F",
      "SEC_STR": "Helix",
      "RSA": "3.2",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.11,
      "dln(kf)_H2O": 0.71,
      "ln(ku)_H2O": -8.52,
      "dln(ku)_H2O": 0.64,
      "ddGKIN_H2O": 0.16,
      "PhiF_H2O": -10.9,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9411",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "I75A",
      "MUTATION_PDB": "I74A",
      "SEC_STR": "Helix",
      "RSA": "10.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -7.95,
      "dln(ku)_H2O": 1.21,
      "ddGKIN_H2O": -5.57,
      "PhiF_H2O": 0.5,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9412",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "I75A",
      "MUTATION_PDB": "I74A",
      "SEC_STR": "Helix",
      "RSA": "10.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.2,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -7.95,
      "dln(ku)_H2O": 1.21,
      "ddGKIN_H2O": -5.57,
      "PhiF_H2O": 0.5,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9412",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "V78A",
      "MUTATION_PDB": "V77A",
      "SEC_STR": "Helix",
      "RSA": "4.9",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.4,
      "dln(kf)_H2O": -2.0,
      "ln(ku)_H2O": -8.38,
      "dln(ku)_H2O": 0.78,
      "ddGKIN_H2O": -6.42,
      "PhiF_H2O": 0.28,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9413",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "V78A",
      "MUTATION_PDB": "V77A",
      "SEC_STR": "Helix",
      "RSA": "4.9",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.4,
      "dln(kf)_H2O": -2.0,
      "ln(ku)_H2O": -8.38,
      "dln(ku)_H2O": 0.78,
      "ddGKIN_H2O": -6.42,
      "PhiF_H2O": 0.28,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9413",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L81A",
      "MUTATION_PDB": "L80A",
      "SEC_STR": "Helix",
      "RSA": "2.4",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.46,
      "dln(kf)_H2O": -2.94,
      "ln(ku)_H2O": -3.87,
      "dln(ku)_H2O": 5.29,
      "ddGKIN_H2O": -19.02,
      "PhiF_H2O": 0.64,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9414",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 86.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L81A",
      "MUTATION_PDB": "L80A",
      "SEC_STR": "Helix",
      "RSA": "2.4",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Sodium Acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 2.46,
      "dln(kf)_H2O": -2.94,
      "ln(ku)_H2O": -3.87,
      "dln(ku)_H2O": 5.29,
      "ddGKIN_H2O": -19.02,
      "PhiF_H2O": 0.64,
      "AUTHOR_KIN": "Kragelund, B.B., Osmark, P., Neergaard, T.B., Schi\u00f8dt, J., Kristiansen, K., Knudsen, J., Poulsen, F.M.",
      "REFERENCE_KIN": "The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nat. Struct. Biol. 6, 594\u2013601. https://doi.org/10.1038/9414",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10360367",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "bACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 79.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I28A",
      "MUTATION_PDB": "I27A",
      "SEC_STR": "Helix",
      "RSA": "9.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.74,
      "dln(kf)_H2O": -1.66,
      "ln(ku)_H2O": -5.89,
      "dln(ku)_H2O": 3.27,
      "dGKIN_H2O": 22.2,
      "ddGKIN_H2O": -11.6,
      "mf": -9.0,
      "mu": 6.36,
      "PhiF_H2O": 0.33,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20358",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "bACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 79.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I28A",
      "MUTATION_PDB": "I27A",
      "SEC_STR": "Helix",
      "RSA": "9.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.74,
      "dln(kf)_H2O": -1.66,
      "ln(ku)_H2O": -5.89,
      "dln(ku)_H2O": 3.27,
      "dGKIN_H2O": 22.2,
      "ddGKIN_H2O": -11.6,
      "mf": -9.0,
      "mu": 6.36,
      "PhiF_H2O": 0.33,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20358",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "bACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 79.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "H31A",
      "MUTATION_PDB": "H30A",
      "SEC_STR": "Helix",
      "RSA": "18.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.45,
      "dln(kf)_H2O": 1.05,
      "ln(ku)_H2O": -3.93,
      "dln(ku)_H2O": 5.23,
      "dGKIN_H2O": 24.0,
      "ddGKIN_H2O": -9.83,
      "mf": -8.96,
      "mu": 4.16,
      "PhiF_H2O": -0.25,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20359",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "bACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 79.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "H31A",
      "MUTATION_PDB": "H30A",
      "SEC_STR": "Helix",
      "RSA": "18.5",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.45,
      "dln(kf)_H2O": 1.05,
      "ln(ku)_H2O": -3.93,
      "dln(ku)_H2O": 5.23,
      "dGKIN_H2O": 24.0,
      "ddGKIN_H2O": -9.83,
      "mf": -8.96,
      "mu": 4.16,
      "PhiF_H2O": -0.25,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20359",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "bACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 79.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y32A",
      "MUTATION_PDB": "Y31A",
      "SEC_STR": "Helix",
      "RSA": "28.8",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.51,
      "dln(kf)_H2O": 0.11,
      "ln(ku)_H2O": -6.1,
      "dln(ku)_H2O": 3.06,
      "dGKIN_H2O": 26.8,
      "ddGKIN_H2O": -7.0,
      "mf": -10.7,
      "mu": 5.52,
      "PhiF_H2O": -0.04,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20360",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "bACBP",
      "SOURCE": "Bos taurus",
      "LENGTH": 79.0,
      "UniProt": "P07107",
      "PDB_wild": "2abd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "2abdA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y32A",
      "MUTATION_PDB": "Y31A",
      "SEC_STR": "Helix",
      "RSA": "28.8",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.51,
      "dln(kf)_H2O": 0.11,
      "ln(ku)_H2O": -6.1,
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      "dGKIN_H2O": 26.8,
      "ddGKIN_H2O": -7.0,
      "mf": -10.7,
      "mu": 5.52,
      "PhiF_H2O": -0.04,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20360",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
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      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
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      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
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      "MUTATION_PDB": "WT(F45W)",
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      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "mf": -6.57,
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi025",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
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      "UniProt": "P0CG48",
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      "pH": 7.4,
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dGKIN_H2O": 30.42,
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi025",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi026",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SEC_STR": "Beta",
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi026",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi027",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi027",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi028",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi028",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SEC_STR": "Beta",
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      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi029",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi029",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "MUTATION_UNIPROT": "T617A",
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      "SEC_STR": "Coil",
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi030",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "MUTATED_CHAIN": "A",
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      "CATH": [
         "1ubqA00 (3.10.20.90)"
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      "MUTATION_UNIPROT": "I621V",
      "MUTATION_PDB": "I13V",
      "SEC_STR": "Beta",
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi031",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I621V",
      "MUTATION_PDB": "I13V",
      "SEC_STR": "Beta",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.03,
      "dln(kf)_H2O": -0.82,
      "ln(ku)_H2O": -4.28,
      "dln(ku)_H2O": 4.88,
      "dGKIN_H2O": 23.07,
      "ddGKIN_H2O": -7.35,
      "mf": -6.59,
      "mu": 2.87,
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      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi031",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I621A",
      "MUTATION_PDB": "I13A",
      "SEC_STR": "Beta",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.4,
      "dln(kf)_H2O": -2.45,
      "ln(ku)_H2O": -2.03,
      "dln(ku)_H2O": 7.13,
      "dGKIN_H2O": 13.45,
      "ddGKIN_H2O": -16.97,
      "mf": -7.18,
      "mu": 2.45,
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      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi032",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I621A",
      "MUTATION_PDB": "I13A",
      "SEC_STR": "Beta",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.4,
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      "ln(ku)_H2O": -2.03,
      "dln(ku)_H2O": 7.13,
      "dGKIN_H2O": 13.45,
      "ddGKIN_H2O": -16.97,
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      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi032",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "L623A",
      "MUTATION_PDB": "L15A",
      "SEC_STR": "Beta",
      "RSA": "4.3",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.2,
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      "ln(ku)_H2O": -2.16,
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      "dGKIN_H2O": 13.28,
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      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi033",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "L623A",
      "MUTATION_PDB": "L15A",
      "SEC_STR": "Beta",
      "RSA": "4.3",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.2,
      "dln(kf)_H2O": -2.65,
      "ln(ku)_H2O": -2.16,
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      "dGKIN_H2O": 13.28,
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      "BACKGROUND_MUT_UNIPROT": [
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi033",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "V625A",
      "MUTATION_PDB": "V17A",
      "SEC_STR": "Coil",
      "RSA": "2.8",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.26,
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      "ln(ku)_H2O": -4.55,
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi034",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
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      "CATH": [
         "1ubqA00 (3.10.20.90)"
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      "MUTATION_UNIPROT": "V625A",
      "MUTATION_PDB": "V17A",
      "SEC_STR": "Coil",
      "RSA": "2.8",
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      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
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         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi034",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "D629N",
      "MUTATION_PDB": "D21N",
      "SEC_STR": "Coil",
      "RSA": "22.7",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
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      "METHOD_KIN": "GuHCl",
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         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi035",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "D629N",
      "MUTATION_PDB": "D21N",
      "SEC_STR": "Coil",
      "RSA": "22.7",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.17,
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      "ln(ku)_H2O": -6.01,
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         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi035",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "T630A",
      "MUTATION_PDB": "T22A",
      "SEC_STR": "Beta",
      "RSA": "33.1",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.22,
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      "ln(ku)_H2O": -4.46,
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      "dGKIN_H2O": 21.51,
      "ddGKIN_H2O": -8.91,
      "mf": -6.79,
      "mu": 3.07,
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      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi036",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "T630A",
      "MUTATION_PDB": "T22A",
      "SEC_STR": "Beta",
      "RSA": "33.1",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.22,
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      "ln(ku)_H2O": -4.46,
      "dln(ku)_H2O": 4.7,
      "dGKIN_H2O": 21.51,
      "ddGKIN_H2O": -8.91,
      "mf": -6.79,
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      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi036",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I631V",
      "MUTATION_PDB": "I23V",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.18,
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      "mf": -6.79,
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         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi037",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I631V",
      "MUTATION_PDB": "I23V",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.18,
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      "dGKIN_H2O": 26.56,
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      "PhiF_H2O": 0.9,
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         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi037",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
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         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I631A",
      "MUTATION_PDB": "I23A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.6,
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      "ln(ku)_H2O": -2.62,
      "dln(ku)_H2O": 6.54,
      "dGKIN_H2O": 17.89,
      "ddGKIN_H2O": -12.53,
      "mf": -7.85,
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      "BACKGROUND_MUT_UNIPROT": [
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi038",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I631A",
      "MUTATION_PDB": "I23A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
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      "pH": 7.4,
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "BACKGROUND_MUT_UNIPROT": [
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi038",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1ubqA00 (3.10.20.90)"
      ],
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      "MUTATION_PDB": "I23G",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
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      ],
      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi039",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I631G",
      "MUTATION_PDB": "I23G",
      "SEC_STR": "Helix",
      "RSA": "0.0",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi039",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
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      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "V634A",
      "MUTATION_PDB": "V26A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi040",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
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      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "V634A",
      "MUTATION_PDB": "V26A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
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      "BUFFER_CONC": "0.05",
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi040",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
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         "1ubqA00 (3.10.20.90)"
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      "MUTATION_UNIPROT": "K635A",
      "MUTATION_PDB": "K27A",
      "SEC_STR": "Helix",
      "RSA": "6.3",
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      "BUFFER_CONC": "0.05",
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi041",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
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         "1ubqA00 (3.10.20.90)"
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      "MUTATION_UNIPROT": "K635A",
      "MUTATION_PDB": "K27A",
      "SEC_STR": "Helix",
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      "BUFFER_CONC": "0.05",
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi041",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "A636G",
      "MUTATION_PDB": "A28G",
      "SEC_STR": "Helix",
      "RSA": "41.5",
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      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      ],
      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi042",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
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      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "A636G",
      "MUTATION_PDB": "A28G",
      "SEC_STR": "Helix",
      "RSA": "41.5",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi042",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I638V",
      "MUTATION_PDB": "I30V",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dGKIN_H2O": 23.51,
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi043",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I638V",
      "MUTATION_PDB": "I30V",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi043",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "I638A",
      "MUTATION_PDB": "I30A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi044",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
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      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi044",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi045",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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         "1ubqA00 (3.10.20.90)"
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      "ddGKIN_H2O": -12.61,
      "mf": -7.09,
      "mu": 3.27,
      "PhiF_H2O": 0.1,
      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi051",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "L675A",
      "MUTATION_PDB": "L67A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.45,
      "dln(kf)_H2O": -0.4,
      "ln(ku)_H2O": -1.74,
      "dln(ku)_H2O": 7.42,
      "dGKIN_H2O": 17.81,
      "ddGKIN_H2O": -12.61,
      "mf": -7.09,
      "mu": 3.27,
      "PhiF_H2O": 0.1,
      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi051",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "L677A",
      "MUTATION_PDB": "L69A",
      "SEC_STR": "Beta",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.32,
      "dln(kf)_H2O": -0.53,
      "ln(ku)_H2O": -1.3,
      "dln(ku)_H2O": 7.86,
      "dGKIN_H2O": 16.4,
      "ddGKIN_H2O": -14.02,
      "mf": -7.38,
      "mu": 2.35,
      "PhiF_H2O": 0.1,
      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi052",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Ubiquitin",
      "SOURCE": "Homo sapiens",
      "LENGTH": 76.0,
      "UniProt": "P0CG48",
      "PDB_wild": "1ubq",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00240"
      ],
      "CATH": [
         "1ubqA00 (3.10.20.90)"
      ],
      "MUTATION_UNIPROT": "L677A",
      "MUTATION_PDB": "L69A",
      "SEC_STR": "Beta",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.4,
      "BUFFER_NAME": "Tris-HCl",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 5.32,
      "dln(kf)_H2O": -0.53,
      "ln(ku)_H2O": -1.3,
      "dln(ku)_H2O": 7.86,
      "dGKIN_H2O": 16.4,
      "ddGKIN_H2O": -14.02,
      "mf": -7.38,
      "mu": 2.35,
      "PhiF_H2O": 0.1,
      "BACKGROUND_MUT_UNIPROT": [
         "F653W"
      ],
      "BACKGROUND_MUT_PDB": [
         "F45W"
      ],
      "AUTHOR_KIN": "Went, H.M., Jackson, S.E.",
      "REFERENCE_KIN": "Ubiquitin folds through a highly polarized transition state. Protein Eng. Des. Sel. 18, 229\u2013237. https://doi.org/10.1093/protein/gzi052",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15857839",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.52,
      "ln(ku)_H2O": -2.53,
      "dGKIN_H2O": 12.5,
      "mf": -3.69,
      "mu": 1.29,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14932",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.52,
      "ln(ku)_H2O": -2.53,
      "dGKIN_H2O": 12.5,
      "mf": -3.69,
      "mu": 1.29,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14932",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D1011G",
      "MUTATION_PDB": "D48G",
      "SEC_STR": "Coil",
      "RSA": "69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.34,
      "dln(kf)_H2O": 3.03,
      "ln(ku)_H2O": -4.51,
      "dln(ku)_H2O": 0.79,
      "dGKIN_H2O": 21.94,
      "ddGKIN_H2O": 5.57,
      "mf": -2.08,
      "mu": 1.06,
      "PhiF_H2O": 1.1,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14897",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D1011G",
      "MUTATION_PDB": "D48G",
      "SEC_STR": "Coil",
      "RSA": "69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.34,
      "dln(kf)_H2O": 3.03,
      "ln(ku)_H2O": -4.51,
      "dln(ku)_H2O": 0.79,
      "dGKIN_H2O": 21.94,
      "ddGKIN_H2O": 5.57,
      "mf": -2.08,
      "mu": 1.06,
      "PhiF_H2O": 1.1,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14897",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L971S,D1011G",
      "MUTATION_PDB": "L8S,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "42.1,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.08,
      "dln(kf)_H2O": 2.77,
      "ln(ku)_H2O": -3.24,
      "dln(ku)_H2O": 2.06,
      "dGKIN_H2O": 18.14,
      "ddGKIN_H2O": -3.8,
      "mf": -2.06,
      "mu": 1.06,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14898",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L971S,D1011G",
      "MUTATION_PDB": "L8S,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "42.1,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.08,
      "dln(kf)_H2O": 2.77,
      "ln(ku)_H2O": -3.24,
      "dln(ku)_H2O": 2.06,
      "dGKIN_H2O": 18.14,
      "ddGKIN_H2O": -3.8,
      "mf": -2.06,
      "mu": 1.06,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14898",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A974G,D1011G",
      "MUTATION_PDB": "A11G,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "1.9,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.26,
      "dln(kf)_H2O": 2.95,
      "ln(ku)_H2O": -0.63,
      "dln(ku)_H2O": 4.67,
      "dGKIN_H2O": 12.13,
      "ddGKIN_H2O": -9.81,
      "mf": -2.3,
      "mu": 0.97,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14899",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A974G,D1011G",
      "MUTATION_PDB": "A11G,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "1.9,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.26,
      "dln(kf)_H2O": 2.95,
      "ln(ku)_H2O": -0.63,
      "dln(ku)_H2O": 4.67,
      "dGKIN_H2O": 12.13,
      "ddGKIN_H2O": -9.81,
      "mf": -2.3,
      "mu": 0.97,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14899",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D977S",
      "MUTATION_PDB": "D14S",
      "SEC_STR": "Coil",
      "RSA": "49.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.06,
      "dln(kf)_H2O": -0.25,
      "ln(ku)_H2O": -3.96,
      "dln(ku)_H2O": 1.34,
      "dGKIN_H2O": 12.46,
      "ddGKIN_H2O": -3.91,
      "mf": -2.21,
      "mu": 1.04,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14900",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D977S",
      "MUTATION_PDB": "D14S",
      "SEC_STR": "Coil",
      "RSA": "49.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.06,
      "dln(kf)_H2O": -0.25,
      "ln(ku)_H2O": -3.96,
      "dln(ku)_H2O": 1.34,
      "dGKIN_H2O": 12.46,
      "ddGKIN_H2O": -3.91,
      "mf": -2.21,
      "mu": 1.04,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14900",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V986A,D1011G",
      "MUTATION_PDB": "V23A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "1.4,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.18,
      "dln(kf)_H2O": 1.87,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 3.0,
      "dGKIN_H2O": 13.58,
      "ddGKIN_H2O": -8.36,
      "mf": -1.88,
      "mu": 1.29,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14901",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V986A,D1011G",
      "MUTATION_PDB": "V23A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "1.4,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.18,
      "dln(kf)_H2O": 1.87,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 3.0,
      "dGKIN_H2O": 13.58,
      "ddGKIN_H2O": -8.36,
      "mf": -1.88,
      "mu": 1.29,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14901",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "T987A,D1011G",
      "MUTATION_PDB": "T24A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "39.4,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.81,
      "dln(kf)_H2O": 2.5,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 17.41,
      "ddGKIN_H2O": -4.53,
      "mf": -2.06,
      "mu": 1.06,
      "PhiF_H2O": 0.29,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14902",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "T987A,D1011G",
      "MUTATION_PDB": "T24A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "39.4,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.81,
      "dln(kf)_H2O": 2.5,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 17.41,
      "ddGKIN_H2O": -4.53,
      "mf": -2.06,
      "mu": 1.06,
      "PhiF_H2O": 0.29,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14902",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D992A,D1011G",
      "MUTATION_PDB": "D29A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "33.1,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.89,
      "dln(kf)_H2O": 2.58,
      "ln(ku)_H2O": -3.0,
      "dln(ku)_H2O": 2.3,
      "dGKIN_H2O": 17.06,
      "ddGKIN_H2O": -4.88,
      "mf": -2.28,
      "mu": 1.14,
      "PhiF_H2O": 0.22,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14903",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D992A,D1011G",
      "MUTATION_PDB": "D29A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "33.1,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.89,
      "dln(kf)_H2O": 2.58,
      "ln(ku)_H2O": -3.0,
      "dln(ku)_H2O": 2.3,
      "dGKIN_H2O": 17.06,
      "ddGKIN_H2O": -4.88,
      "mf": -2.28,
      "mu": 1.14,
      "PhiF_H2O": 0.22,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14903",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L996V,D1011G",
      "MUTATION_PDB": "L33V,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "6.1,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.85,
      "dln(kf)_H2O": 3.54,
      "ln(ku)_H2O": -2.21,
      "dln(ku)_H2O": 3.09,
      "dGKIN_H2O": 17.49,
      "ddGKIN_H2O": -4.45,
      "mf": -1.93,
      "mu": 1.16,
      "PhiF_H2O": -0.2,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14904",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L996V,D1011G",
      "MUTATION_PDB": "L33V,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "6.1,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.85,
      "dln(kf)_H2O": 3.54,
      "ln(ku)_H2O": -2.21,
      "dln(ku)_H2O": 3.09,
      "dGKIN_H2O": 17.49,
      "ddGKIN_H2O": -4.45,
      "mf": -1.93,
      "mu": 1.16,
      "PhiF_H2O": -0.2,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14904",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "S999N,D1011G",
      "MUTATION_PDB": "S36N,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "34.6,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.87,
      "dln(kf)_H2O": 2.56,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 17.57,
      "ddGKIN_H2O": -4.37,
      "mf": -2.28,
      "mu": 0.89,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14905",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "S999N,D1011G",
      "MUTATION_PDB": "S36N,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "34.6,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.87,
      "dln(kf)_H2O": 2.56,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 17.57,
      "ddGKIN_H2O": -4.37,
      "mf": -2.28,
      "mu": 0.89,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14905",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "K1006A,D1011G",
      "MUTATION_PDB": "K43A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "31.2,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.91,
      "dln(kf)_H2O": 2.6,
      "ln(ku)_H2O": -3.32,
      "dln(ku)_H2O": 1.98,
      "dGKIN_H2O": 17.93,
      "ddGKIN_H2O": -4.01,
      "mf": -2.13,
      "mu": 1.06,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14906",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "K1006A,D1011G",
      "MUTATION_PDB": "K43A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "31.2,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.91,
      "dln(kf)_H2O": 2.6,
      "ln(ku)_H2O": -3.32,
      "dln(ku)_H2O": 1.98,
      "dGKIN_H2O": 17.93,
      "ddGKIN_H2O": -4.01,
      "mf": -2.13,
      "mu": 1.06,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14906",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1007A,D1011G",
      "MUTATION_PDB": "V44A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.61,
      "dln(kf)_H2O": 0.3,
      "ln(ku)_H2O": -1.51,
      "dln(ku)_H2O": 3.79,
      "dGKIN_H2O": 7.74,
      "ddGKIN_H2O": -14.2,
      "mf": -2.63,
      "mu": 1.04,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14907",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1007A,D1011G",
      "MUTATION_PDB": "V44A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.61,
      "dln(kf)_H2O": 0.3,
      "ln(ku)_H2O": -1.51,
      "dln(ku)_H2O": 3.79,
      "dGKIN_H2O": 7.74,
      "ddGKIN_H2O": -14.2,
      "mf": -2.63,
      "mu": 1.04,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14907",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1009A,D1011G",
      "MUTATION_PDB": "V46A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "12.0,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.42,
      "dln(kf)_H2O": 1.11,
      "ln(ku)_H2O": -4.96,
      "dln(ku)_H2O": 0.34,
      "dGKIN_H2O": 18.3,
      "ddGKIN_H2O": -3.64,
      "mf": -2.21,
      "mu": 1.06,
      "PhiF_H2O": 1.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14908",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1009A,D1011G",
      "MUTATION_PDB": "V46A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "12.0,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.42,
      "dln(kf)_H2O": 1.11,
      "ln(ku)_H2O": -4.96,
      "dln(ku)_H2O": 0.34,
      "dGKIN_H2O": 18.3,
      "ddGKIN_H2O": -3.64,
      "mf": -2.21,
      "mu": 1.06,
      "PhiF_H2O": 1.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14908",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "N1010G",
      "MUTATION_PDB": "N47G",
      "SEC_STR": "Coil",
      "RSA": "93.6",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.69,
      "dln(kf)_H2O": 0.38,
      "ln(ku)_H2O": -5.52,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 17.86,
      "ddGKIN_H2O": 1.49,
      "mf": -2.21,
      "mu": 1.06,
      "PhiF_H2O": 0.63,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14909",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "N1010G",
      "MUTATION_PDB": "N47G",
      "SEC_STR": "Coil",
      "RSA": "93.6",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.69,
      "dln(kf)_H2O": 0.38,
      "ln(ku)_H2O": -5.52,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 17.86,
      "ddGKIN_H2O": 1.49,
      "mf": -2.21,
      "mu": 1.06,
      "PhiF_H2O": 0.63,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14909",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "F1015A,D1011G",
      "MUTATION_PDB": "F52A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "28.4,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.7,
      "dln(kf)_H2O": 0.39,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": 2.64,
      "dGKIN_H2O": 10.81,
      "ddGKIN_H2O": -11.13,
      "mf": -2.48,
      "mu": 0.84,
      "PhiF_H2O": 0.58,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14910",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "F1015A,D1011G",
      "MUTATION_PDB": "F52A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "28.4,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.7,
      "dln(kf)_H2O": 0.39,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": 2.64,
      "dGKIN_H2O": 10.81,
      "ddGKIN_H2O": -11.13,
      "mf": -2.48,
      "mu": 0.84,
      "PhiF_H2O": 0.58,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14910",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1016A,D1011G",
      "MUTATION_PDB": "V53A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.08,
      "dln(kf)_H2O": 0.77,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 13.13,
      "ddGKIN_H2O": -8.81,
      "mf": -2.3,
      "mu": 1.19,
      "PhiF_H2O": 0.61,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14911",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1016A,D1011G",
      "MUTATION_PDB": "V53A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.08,
      "dln(kf)_H2O": 0.77,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 13.13,
      "ddGKIN_H2O": -8.81,
      "mf": -2.3,
      "mu": 1.19,
      "PhiF_H2O": 0.61,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14911",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A1018G,D1011G",
      "MUTATION_PDB": "A55G,D48G",
      "SEC_STR": "Helix,Coil",
      "RSA": "13.2,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.56,
      "dln(kf)_H2O": 1.25,
      "ln(ku)_H2O": -3.0,
      "dln(ku)_H2O": 2.3,
      "dGKIN_H2O": 13.76,
      "ddGKIN_H2O": -8.18,
      "mf": -2.38,
      "mu": 1.04,
      "PhiF_H2O": 0.53,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14912",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A1018G,D1011G",
      "MUTATION_PDB": "A55G,D48G",
      "SEC_STR": "Helix,Coil",
      "RSA": "13.2,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.56,
      "dln(kf)_H2O": 1.25,
      "ln(ku)_H2O": -3.0,
      "dln(ku)_H2O": 2.3,
      "dGKIN_H2O": 13.76,
      "ddGKIN_H2O": -8.18,
      "mf": -2.38,
      "mu": 1.04,
      "PhiF_H2O": 0.53,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14912",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1021A,D1011G",
      "MUTATION_PDB": "V58A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "8.5,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.71,
      "dln(kf)_H2O": 2.4,
      "ln(ku)_H2O": -1.14,
      "dln(ku)_H2O": 4.16,
      "dGKIN_H2O": 12.02,
      "ddGKIN_H2O": -9.92,
      "mf": -2.38,
      "mu": 1.11,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14913",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1021A,D1011G",
      "MUTATION_PDB": "V58A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "8.5,69.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.71,
      "dln(kf)_H2O": 2.4,
      "ln(ku)_H2O": -1.14,
      "dln(ku)_H2O": 4.16,
      "dGKIN_H2O": 12.02,
      "ddGKIN_H2O": -9.92,
      "mf": -2.38,
      "mu": 1.11,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14913",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D1011G",
      "MUTATION_PDB": "D48G",
      "SEC_STR": "Coil",
      "RSA": "69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.91,
      "dln(kf)_H2O": 1.39,
      "ln(ku)_H2O": -2.53,
      "dGKIN_H2O": 15.95,
      "ddGKIN_H2O": 3.45,
      "mf": -2.97,
      "mu": 1.24,
      "PhiF_H2O": 1.0,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14933",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D1011G",
      "MUTATION_PDB": "D48G",
      "SEC_STR": "Coil",
      "RSA": "69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.91,
      "dln(kf)_H2O": 1.39,
      "ln(ku)_H2O": -2.53,
      "dGKIN_H2O": 15.95,
      "ddGKIN_H2O": 3.45,
      "mf": -2.97,
      "mu": 1.24,
      "PhiF_H2O": 1.0,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14933",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L971S,D1011G",
      "MUTATION_PDB": "L8S,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "42.1,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.81,
      "dln(kf)_H2O": 1.29,
      "ln(ku)_H2O": -1.27,
      "dln(ku)_H2O": 1.26,
      "dGKIN_H2O": 12.59,
      "ddGKIN_H2O": -3.36,
      "mf": -3.39,
      "mu": 1.19,
      "PhiF_H2O": 0.07,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14934",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L971S,D1011G",
      "MUTATION_PDB": "L8S,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "42.1,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.81,
      "dln(kf)_H2O": 1.29,
      "ln(ku)_H2O": -1.27,
      "dln(ku)_H2O": 1.26,
      "dGKIN_H2O": 12.59,
      "ddGKIN_H2O": -3.36,
      "mf": -3.39,
      "mu": 1.19,
      "PhiF_H2O": 0.07,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14934",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A974G,D1011G",
      "MUTATION_PDB": "A11G,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "1.9,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.76,
      "dln(kf)_H2O": 1.24,
      "ln(ku)_H2O": 0.34,
      "dln(ku)_H2O": 2.87,
      "dGKIN_H2O": 8.47,
      "ddGKIN_H2O": -7.48,
      "mf": -3.12,
      "mu": 1.26,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14935",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A974G,D1011G",
      "MUTATION_PDB": "A11G,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "1.9,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.76,
      "dln(kf)_H2O": 1.24,
      "ln(ku)_H2O": 0.34,
      "dln(ku)_H2O": 2.87,
      "dGKIN_H2O": 8.47,
      "ddGKIN_H2O": -7.48,
      "mf": -3.12,
      "mu": 1.26,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14935",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D977S",
      "MUTATION_PDB": "D14S",
      "SEC_STR": "Coil",
      "RSA": "49.1",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.44,
      "dln(kf)_H2O": -0.08,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": -0.13,
      "dGKIN_H2O": 12.64,
      "ddGKIN_H2O": 0.14,
      "mf": -2.97,
      "mu": 1.39,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14936",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D977S",
      "MUTATION_PDB": "D14S",
      "SEC_STR": "Coil",
      "RSA": "49.1",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.44,
      "dln(kf)_H2O": -0.08,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": -0.13,
      "dGKIN_H2O": 12.64,
      "ddGKIN_H2O": 0.14,
      "mf": -2.97,
      "mu": 1.39,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14936",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V986A,D1011G",
      "MUTATION_PDB": "V23A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "1.4,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.18,
      "dln(kf)_H2O": 0.66,
      "ln(ku)_H2O": -0.51,
      "dln(ku)_H2O": 2.02,
      "dGKIN_H2O": 9.14,
      "ddGKIN_H2O": -6.81,
      "mf": -3.42,
      "mu": 1.36,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14937",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V986A,D1011G",
      "MUTATION_PDB": "V23A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "1.4,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.18,
      "dln(kf)_H2O": 0.66,
      "ln(ku)_H2O": -0.51,
      "dln(ku)_H2O": 2.02,
      "dGKIN_H2O": 9.14,
      "ddGKIN_H2O": -6.81,
      "mf": -3.42,
      "mu": 1.36,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14937",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "T987A,D1011G",
      "MUTATION_PDB": "T24A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "39.4,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.5,
      "dln(kf)_H2O": 0.98,
      "ln(ku)_H2O": -1.24,
      "dln(ku)_H2O": 1.29,
      "dGKIN_H2O": 11.73,
      "ddGKIN_H2O": -4.22,
      "mf": -2.82,
      "mu": 1.24,
      "PhiF_H2O": 0.24,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14938",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "T987A,D1011G",
      "MUTATION_PDB": "T24A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "39.4,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.5,
      "dln(kf)_H2O": 0.98,
      "ln(ku)_H2O": -1.24,
      "dln(ku)_H2O": 1.29,
      "dGKIN_H2O": 11.73,
      "ddGKIN_H2O": -4.22,
      "mf": -2.82,
      "mu": 1.24,
      "PhiF_H2O": 0.24,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14938",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D992A,D1011G",
      "MUTATION_PDB": "D29A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "33.1,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.61,
      "dln(kf)_H2O": 1.09,
      "ln(ku)_H2O": -1.66,
      "dln(ku)_H2O": 0.87,
      "dGKIN_H2O": 13.06,
      "ddGKIN_H2O": -2.89,
      "mf": -3.12,
      "mu": 1.54,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14939",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "D992A,D1011G",
      "MUTATION_PDB": "D29A,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "33.1,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.61,
      "dln(kf)_H2O": 1.09,
      "ln(ku)_H2O": -1.66,
      "dln(ku)_H2O": 0.87,
      "dGKIN_H2O": 13.06,
      "ddGKIN_H2O": -2.89,
      "mf": -3.12,
      "mu": 1.54,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14939",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L996V,D1011G",
      "MUTATION_PDB": "L33V,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "6.1,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.44,
      "dln(kf)_H2O": 1.92,
      "ln(ku)_H2O": -0.45,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 12.11,
      "ddGKIN_H2O": -3.84,
      "mf": -3.1,
      "mu": 1.21,
      "PhiF_H2O": -0.3,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14940",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "L996V,D1011G",
      "MUTATION_PDB": "L33V,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "6.1,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.44,
      "dln(kf)_H2O": 1.92,
      "ln(ku)_H2O": -0.45,
      "dln(ku)_H2O": 2.08,
      "dGKIN_H2O": 12.11,
      "ddGKIN_H2O": -3.84,
      "mf": -3.1,
      "mu": 1.21,
      "PhiF_H2O": -0.3,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14940",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "S999N,D1011G",
      "MUTATION_PDB": "S36N,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "34.6,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.78,
      "dln(kf)_H2O": 1.26,
      "ln(ku)_H2O": -1.61,
      "dln(ku)_H2O": 0.92,
      "dGKIN_H2O": 13.36,
      "ddGKIN_H2O": -2.59,
      "mf": -2.92,
      "mu": 1.24,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14941",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "S999N,D1011G",
      "MUTATION_PDB": "S36N,D48G",
      "SEC_STR": "Coil,Coil",
      "RSA": "34.6,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.78,
      "dln(kf)_H2O": 1.26,
      "ln(ku)_H2O": -1.61,
      "dln(ku)_H2O": 0.92,
      "dGKIN_H2O": 13.36,
      "ddGKIN_H2O": -2.59,
      "mf": -2.92,
      "mu": 1.24,
      "PhiF_H2O": 0.12,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14941",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "K1006A,D1011G",
      "MUTATION_PDB": "K43A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "31.2,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.64,
      "dln(kf)_H2O": 1.12,
      "ln(ku)_H2O": -1.71,
      "dln(ku)_H2O": 0.82,
      "dGKIN_H2O": 13.26,
      "ddGKIN_H2O": -2.69,
      "mf": -2.8,
      "mu": 1.31,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14942",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "K1006A,D1011G",
      "MUTATION_PDB": "K43A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "31.2,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.64,
      "dln(kf)_H2O": 1.12,
      "ln(ku)_H2O": -1.71,
      "dln(ku)_H2O": 0.82,
      "dGKIN_H2O": 13.26,
      "ddGKIN_H2O": -2.69,
      "mf": -2.8,
      "mu": 1.31,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14942",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1007A,D1011G",
      "MUTATION_PDB": "V44A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.1,
      "dln(kf)_H2O": -1.42,
      "ln(ku)_H2O": 0.12,
      "dln(ku)_H2O": 2.65,
      "dGKIN_H2O": 2.42,
      "ddGKIN_H2O": -13.53,
      "mf": -2.97,
      "mu": 1.24,
      "PhiF_H2O": 0.52,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14943",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1007A,D1011G",
      "MUTATION_PDB": "V44A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.1,
      "dln(kf)_H2O": -1.42,
      "ln(ku)_H2O": 0.12,
      "dln(ku)_H2O": 2.65,
      "dGKIN_H2O": 2.42,
      "ddGKIN_H2O": -13.53,
      "mf": -2.97,
      "mu": 1.24,
      "PhiF_H2O": 0.52,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14943",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1009A,D1011G",
      "MUTATION_PDB": "V46A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "12.0,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.17,
      "dln(kf)_H2O": -0.35,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": -0.13,
      "dGKIN_H2O": 11.98,
      "ddGKIN_H2O": -3.97,
      "mf": -3.0,
      "mu": 1.07,
      "PhiF_H2O": 1.1,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14944",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1009A,D1011G",
      "MUTATION_PDB": "V46A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "12.0,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.17,
      "dln(kf)_H2O": -0.35,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": -0.13,
      "dGKIN_H2O": 11.98,
      "ddGKIN_H2O": -3.97,
      "mf": -3.0,
      "mu": 1.07,
      "PhiF_H2O": 1.1,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14944",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "N1010G",
      "MUTATION_PDB": "N47G",
      "SEC_STR": "Coil",
      "RSA": "93.6",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.89,
      "dln(kf)_H2O": 0.37,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.69,
      "dGKIN_H2O": 15.14,
      "ddGKIN_H2O": 2.64,
      "mf": -3.15,
      "mu": 1.39,
      "PhiF_H2O": 0.69,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14945",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "N1010G",
      "MUTATION_PDB": "N47G",
      "SEC_STR": "Coil",
      "RSA": "93.6",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 2.89,
      "dln(kf)_H2O": 0.37,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.69,
      "dGKIN_H2O": 15.14,
      "ddGKIN_H2O": 2.64,
      "mf": -3.15,
      "mu": 1.39,
      "PhiF_H2O": 0.69,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14945",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "F1015A,D1011G",
      "MUTATION_PDB": "F52A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "28.4,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.16,
      "dln(kf)_H2O": -1.36,
      "ln(ku)_H2O": -0.97,
      "dln(ku)_H2O": 1.56,
      "dGKIN_H2O": 5.28,
      "ddGKIN_H2O": -10.67,
      "mf": -2.97,
      "mu": 1.14,
      "PhiF_H2O": 0.64,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14946",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "F1015A,D1011G",
      "MUTATION_PDB": "F52A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "28.4,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.16,
      "dln(kf)_H2O": -1.36,
      "ln(ku)_H2O": -0.97,
      "dln(ku)_H2O": 1.56,
      "dGKIN_H2O": 5.28,
      "ddGKIN_H2O": -10.67,
      "mf": -2.97,
      "mu": 1.14,
      "PhiF_H2O": 0.64,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14946",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1016A,D1011G",
      "MUTATION_PDB": "V53A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.96,
      "dln(kf)_H2O": -1.56,
      "ln(ku)_H2O": -0.73,
      "dln(ku)_H2O": 1.8,
      "dGKIN_H2O": 4.19,
      "ddGKIN_H2O": -11.76,
      "mf": -2.97,
      "mu": 1.26,
      "PhiF_H2O": 0.62,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14947",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1016A,D1011G",
      "MUTATION_PDB": "V53A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "0.0,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.96,
      "dln(kf)_H2O": -1.56,
      "ln(ku)_H2O": -0.73,
      "dln(ku)_H2O": 1.8,
      "dGKIN_H2O": 4.19,
      "ddGKIN_H2O": -11.76,
      "mf": -2.97,
      "mu": 1.26,
      "PhiF_H2O": 0.62,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14947",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A1018G,D1011G",
      "MUTATION_PDB": "A55G,D48G",
      "SEC_STR": "Helix,Coil",
      "RSA": "13.2,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.59,
      "dln(kf)_H2O": -0.93,
      "ln(ku)_H2O": -1.43,
      "dln(ku)_H2O": 1.1,
      "dGKIN_H2O": 7.47,
      "ddGKIN_H2O": -8.48,
      "mf": -2.6,
      "mu": 1.31,
      "PhiF_H2O": 0.68,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14948",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "A1018G,D1011G",
      "MUTATION_PDB": "A55G,D48G",
      "SEC_STR": "Helix,Coil",
      "RSA": "13.2,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.59,
      "dln(kf)_H2O": -0.93,
      "ln(ku)_H2O": -1.43,
      "dln(ku)_H2O": 1.1,
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      "ddGKIN_H2O": -8.48,
      "mf": -2.6,
      "mu": 1.31,
      "PhiF_H2O": 0.68,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14948",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1021A,D1011G",
      "MUTATION_PDB": "V58A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "8.5,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.14,
      "dln(kf)_H2O": 0.62,
      "ln(ku)_H2O": 0.22,
      "dln(ku)_H2O": 2.75,
      "dGKIN_H2O": 7.24,
      "ddGKIN_H2O": -8.71,
      "mf": -3.07,
      "mu": 1.46,
      "PhiF_H2O": 0.22,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14949",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "V1021A,D1011G",
      "MUTATION_PDB": "V58A,D48G",
      "SEC_STR": "Beta,Coil",
      "RSA": "8.5,69.3",
      "T": 25.0,
      "pH": 3.5,
      "BUFFER_NAME": "Glycine",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 3.14,
      "dln(kf)_H2O": 0.62,
      "ln(ku)_H2O": 0.22,
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      "dGKIN_H2O": 7.24,
      "ddGKIN_H2O": -8.71,
      "mf": -3.07,
      "mu": 1.46,
      "PhiF_H2O": 0.22,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14949",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.31,
      "ln(ku)_H2O": -5.3,
      "dGKIN_H2O": 16.37,
      "mf": -2.18,
      "mu": 1.07,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14896",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Spectrin SH3",
      "SOURCE": "Gallus gallus",
      "LENGTH": 62.0,
      "UniProt": "P07751",
      "PDB_wild": "1shg",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00018"
      ],
      "CATH": [
         "1shgA00 (2.30.30.40)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 1.31,
      "ln(ku)_H2O": -5.3,
      "dGKIN_H2O": 16.37,
      "mf": -2.18,
      "mu": 1.07,
      "AUTHOR_KIN": "Mart\u00ednez, J.C., Serrano, L.",
      "REFERENCE_KIN": "The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010\u20131016. https://doi.org/10.1038/14896",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542091",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -1.42,
      "ln(ku)_H2O": -9.64,
      "dGKIN_H2O": 20.6,
      "mf": -4.2,
      "mu": 1.25,
      "CM_KIN": 3.77,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14890",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -1.42,
      "ln(ku)_H2O": -9.64,
      "dGKIN_H2O": 20.6,
      "mf": -4.2,
      "mu": 1.25,
      "CM_KIN": 3.77,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14890",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "Y12F",
      "MUTATION_PDB": "Y12F",
      "SEC_STR": "Beta",
      "RSA": "0.9",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.12,
      "dln(kf)_H2O": 1.3,
      "ln(ku)_H2O": -9.35,
      "dln(ku)_H2O": 0.29,
      "ddGKIN_H2O": 2.5,
      "mf": -3.38,
      "mu": 1.0,
      "CM_KIN": 5.27,
      "PhiF_H2O": 0.93,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14891",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "Y12F",
      "MUTATION_PDB": "Y12F",
      "SEC_STR": "Beta",
      "RSA": "0.9",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -0.12,
      "dln(kf)_H2O": 1.3,
      "ln(ku)_H2O": -9.35,
      "dln(ku)_H2O": 0.29,
      "ddGKIN_H2O": 2.5,
      "mf": -3.38,
      "mu": 1.0,
      "CM_KIN": 5.27,
      "PhiF_H2O": 0.93,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14891",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "Y12I",
      "MUTATION_PDB": "Y12I",
      "SEC_STR": "Beta",
      "RSA": "0.9",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -4.15,
      "dln(kf)_H2O": -2.73,
      "ln(ku)_H2O": -9.09,
      "dln(ku)_H2O": 0.55,
      "ddGKIN_H2O": -8.25,
      "mf": -4.25,
      "mu": 1.33,
      "CM_KIN": 2.22,
      "PhiF_H2O": 0.83,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14892",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "Y12I",
      "MUTATION_PDB": "Y12I",
      "SEC_STR": "Beta",
      "RSA": "0.9",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -4.15,
      "dln(kf)_H2O": -2.73,
      "ln(ku)_H2O": -9.09,
      "dln(ku)_H2O": 0.55,
      "ddGKIN_H2O": -8.25,
      "mf": -4.25,
      "mu": 1.33,
      "CM_KIN": 2.22,
      "PhiF_H2O": 0.83,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14892",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "V14A",
      "MUTATION_PDB": "V14A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -3.02,
      "dln(kf)_H2O": -1.6,
      "ln(ku)_H2O": -6.93,
      "dln(ku)_H2O": 2.71,
      "ddGKIN_H2O": -10.85,
      "mf": -3.83,
      "mu": 1.3,
      "CM_KIN": 1.91,
      "PhiF_H2O": 0.37,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14893",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "V14A",
      "MUTATION_PDB": "V14A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": -3.02,
      "dln(kf)_H2O": -1.6,
      "ln(ku)_H2O": -6.93,
      "dln(ku)_H2O": 2.71,
      "ddGKIN_H2O": -10.85,
      "mf": -3.83,
      "mu": 1.3,
      "CM_KIN": 1.91,
      "PhiF_H2O": 0.37,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14893",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "V18A",
      "MUTATION_PDB": "V18A",
      "SEC_STR": "Coil",
      "RSA": "1.4",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dln(kf)_H2O": -0.31,
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      "ddGKIN_H2O": -7.4,
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      "PhiF_H2O": 0.1,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14894",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
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      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "V18A",
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      "SEC_STR": "Coil",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PMID_KIN": "10542090",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "mAcP",
      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
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      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
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      "PMID_KIN": "10542090",
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      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14913",
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      "PMID_KIN": "10542090",
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      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14916",
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      "PMID_KIN": "10542090",
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      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14916",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_UNIPROT": "F95L",
      "MUTATION_PDB": "F95L",
      "SEC_STR": "Beta",
      "RSA": "7.1",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(ku)_H2O": -7.91,
      "dln(ku)_H2O": 1.73,
      "mu": -1.13,
      "PhiF_H2O": 0.76,
      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14917",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Homo sapiens",
      "LENGTH": 98.0,
      "UniProt": "P14621",
      "PDB_wild": "AF-P14621",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "EC_NUMBER": "3.6.1.7",
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      "MUTATION_PDB": "F95L",
      "SEC_STR": "Beta",
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      "pH": 5.5,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dln(ku)_H2O": 1.73,
      "mu": -1.13,
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      "AUTHOR_KIN": "Chiti, F., Taddei, N., White, P.M., Bucciantini, M., Magherini, F., Stefani, M., Dobson, C.M.",
      "REFERENCE_KIN": "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat. Struct. Biol. 6, 1005\u20131009. https://doi.org/10.1038/14917",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10542090",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
      "UniProt": "P01053",
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      "MUTATED_CHAIN": "I",
      "PFAM": [
         "PF00280"
      ],
      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "L52A,V58A,F70L",
      "MUTATION_PDB": "L51A,V57A,F69L",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "dln(kf)_H2O": -1.56,
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      "dGKIN_H2O": 18.66,
      "mf": -5.95,
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      "AUTHOR_KIN": "Itzhaki LS, Otzen DE, Fersht AR",
      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
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         "PF00280"
      ],
      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
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      "MEASURE_KIN": "stopped-flow",
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      "dGKIN_H2O": 18.66,
      "mf": -5.95,
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Hordeum vulgare",
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      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "AUTHOR_KIN": "Itzhaki LS, Otzen DE, Fersht AR",
      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
      "UniProt": "P01053",
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      "MUTATED_CHAIN": "I",
      "PFAM": [
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      ],
      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "L52V,V58A,F70L",
      "MUTATION_PDB": "L51V,V57A,F69L",
      "SEC_STR": "Beta,Coil,Beta",
      "RSA": "23.8,40.8,16.2",
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      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Hordeum vulgare",
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      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "V54T",
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      "BUFFER_NAME": "MES",
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
      "UniProt": "P01053",
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      "MUTATED_CHAIN": "I",
      "PFAM": [
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      ],
      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "V54T",
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      "SEC_STR": "Coil",
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      "BUFFER_NAME": "MES",
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Hordeum vulgare",
      "LENGTH": 83.0,
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      "MUTATED_CHAIN": "I",
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      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "V54A",
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
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      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Hordeum vulgare",
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         "1coaI00 (3.30.10.10)"
      ],
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
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      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Hordeum vulgare",
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      ],
      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
      "MUTATION_UNIPROT": "V54G",
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Hordeum vulgare",
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         "1coaI00 (3.30.10.10)"
      ],
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
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      "SOURCE": "Hordeum vulgare",
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         "1coaI00 (3.30.10.10)"
      ],
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
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      "PMID_KIN": "7490748",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
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      "CATH": [
         "1coaI00 (3.30.10.10)"
      ],
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      "AUTHOR_KIN": "Itzhaki LS, Otzen DE, Fersht AR",
      "REFERENCE_KIN": "The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding,  J Mol Biol. 254(2):260-288. doi: 10.1006/jmbi.1995.0616.",
      "YEAR_KIN": 1995.0,
      "PMID_KIN": "7490748",
      "STATE": "2",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.12,
      "mu": 1.38,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77971",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.12,
      "mu": 1.38,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77971",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y229L",
      "MUTATION_PDB": "Y3L",
      "SEC_STR": "Beta",
      "RSA": "5.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.23,
      "mu": 1.38,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77972",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y229L",
      "MUTATION_PDB": "Y3L",
      "SEC_STR": "Beta",
      "RSA": "5.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.23,
      "mu": 1.38,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77972",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I232A",
      "MUTATION_PDB": "I6A",
      "SEC_STR": "Beta",
      "RSA": "37.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.85,
      "mu": 1.38,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77973",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "I232A",
      "MUTATION_PDB": "I6A",
      "SEC_STR": "Beta",
      "RSA": "37.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.85,
      "mu": 1.38,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77973",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L233A",
      "MUTATION_PDB": "L7A",
      "SEC_STR": "Beta",
      "RSA": "4.3",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.62,
      "mu": 1.59,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77974",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "L233A",
      "MUTATION_PDB": "L7A",
      "SEC_STR": "Beta",
      "RSA": "4.3",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.62,
      "mu": 1.59,
      "PhiF_H2O": 0.32,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77974",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T237A",
      "MUTATION_PDB": "T11A",
      "SEC_STR": "Coil",
      "RSA": "90.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.26,
      "mu": 2.18,
      "PhiF_H2O": 0.02,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77975",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T237A",
      "MUTATION_PDB": "T11A",
      "SEC_STR": "Coil",
      "RSA": "90.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.26,
      "mu": 2.18,
      "PhiF_H2O": 0.02,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77975",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E241A",
      "MUTATION_PDB": "E15A",
      "SEC_STR": "Beta",
      "RSA": "60.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.55,
      "mu": 1.92,
      "PhiF_H2O": -0.19,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77976",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "E241A",
      "MUTATION_PDB": "E15A",
      "SEC_STR": "Beta",
      "RSA": "60.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.55,
      "mu": 1.92,
      "PhiF_H2O": -0.19,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77976",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T242A",
      "MUTATION_PDB": "T16A",
      "SEC_STR": "Beta",
      "RSA": "33.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.98,
      "mu": 1.51,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77977",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T242A",
      "MUTATION_PDB": "T16A",
      "SEC_STR": "Beta",
      "RSA": "33.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.98,
      "mu": 1.51,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77977",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T244A",
      "MUTATION_PDB": "T18A",
      "SEC_STR": "Beta",
      "RSA": "26.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.22,
      "mu": 1.63,
      "PhiF_H2O": -0.45,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77978",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T244A",
      "MUTATION_PDB": "T18A",
      "SEC_STR": "Beta",
      "RSA": "26.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.22,
      "mu": 1.63,
      "PhiF_H2O": -0.45,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77978",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A246G",
      "MUTATION_PDB": "A20G",
      "SEC_STR": "Coil",
      "RSA": "13.2",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.84,
      "mu": 2.01,
      "PhiF_H2O": 0.02,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77979",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A246G",
      "MUTATION_PDB": "A20G",
      "SEC_STR": "Coil",
      "RSA": "13.2",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.84,
      "mu": 2.01,
      "PhiF_H2O": 0.02,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77979",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D248A",
      "MUTATION_PDB": "D22A",
      "SEC_STR": "Coil",
      "RSA": "42.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.74,
      "mu": 2.05,
      "PhiF_H2O": 0.23,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77980",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D248A",
      "MUTATION_PDB": "D22A",
      "SEC_STR": "Coil",
      "RSA": "42.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.74,
      "mu": 2.05,
      "PhiF_H2O": 0.23,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77980",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T251A",
      "MUTATION_PDB": "T25A",
      "SEC_STR": "Helix",
      "RSA": "30.3",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.74,
      "mu": 1.55,
      "PhiF_H2O": -0.81,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77981",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T251A",
      "MUTATION_PDB": "T25A",
      "SEC_STR": "Helix",
      "RSA": "30.3",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.74,
      "mu": 1.55,
      "PhiF_H2O": -0.81,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77981",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A252G",
      "MUTATION_PDB": "A26G",
      "SEC_STR": "Helix",
      "RSA": "0.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -10.3,
      "mu": 1.34,
      "PhiF_H2O": 0.31,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77982",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A252G",
      "MUTATION_PDB": "A26G",
      "SEC_STR": "Helix",
      "RSA": "0.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -10.3,
      "mu": 1.34,
      "PhiF_H2O": 0.31,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77982",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K254G",
      "MUTATION_PDB": "K28G",
      "SEC_STR": "Helix",
      "RSA": "59.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.22,
      "mu": 1.88,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77983",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K254G",
      "MUTATION_PDB": "K28G",
      "SEC_STR": "Helix",
      "RSA": "59.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.22,
      "mu": 1.88,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77983",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V255A",
      "MUTATION_PDB": "V29A",
      "SEC_STR": "Helix",
      "RSA": "50.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.69,
      "mu": 1.84,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77984",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V255A",
      "MUTATION_PDB": "V29A",
      "SEC_STR": "Helix",
      "RSA": "50.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.69,
      "mu": 1.84,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77984",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F256L",
      "MUTATION_PDB": "F30L",
      "SEC_STR": "Helix",
      "RSA": "2.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.74,
      "mu": 1.8,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77985",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F256L",
      "MUTATION_PDB": "F30L",
      "SEC_STR": "Helix",
      "RSA": "2.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.74,
      "mu": 1.8,
      "PhiF_H2O": 0.05,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77985",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K257G",
      "MUTATION_PDB": "K31G",
      "SEC_STR": "Helix",
      "RSA": "41.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.98,
      "mu": 1.55,
      "PhiF_H2O": 0.23,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77986",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "K257G",
      "MUTATION_PDB": "K31G",
      "SEC_STR": "Helix",
      "RSA": "41.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.98,
      "mu": 1.55,
      "PhiF_H2O": 0.23,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77986",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Q258G",
      "MUTATION_PDB": "Q32G",
      "SEC_STR": "Helix",
      "RSA": "66.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.69,
      "mu": 1.59,
      "PhiF_H2O": 0.55,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77987",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Q258G",
      "MUTATION_PDB": "Q32G",
      "SEC_STR": "Helix",
      "RSA": "66.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.69,
      "mu": 1.59,
      "PhiF_H2O": 0.55,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77987",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y259A",
      "MUTATION_PDB": "Y33A",
      "SEC_STR": "Helix",
      "RSA": "34.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.21,
      "mu": 2.26,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77988",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y259A",
      "MUTATION_PDB": "Y33A",
      "SEC_STR": "Helix",
      "RSA": "34.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.21,
      "mu": 2.26,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77988",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A260G",
      "MUTATION_PDB": "A34G",
      "SEC_STR": "Helix",
      "RSA": "1.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.46,
      "mu": 1.76,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77989",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "A260G",
      "MUTATION_PDB": "A34G",
      "SEC_STR": "Helix",
      "RSA": "1.9",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.46,
      "mu": 1.76,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77989",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N261G",
      "MUTATION_PDB": "N35G",
      "SEC_STR": "Helix",
      "RSA": "77.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.41,
      "mu": 1.67,
      "PhiF_H2O": 0.19,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77990",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N261G",
      "MUTATION_PDB": "N35G",
      "SEC_STR": "Helix",
      "RSA": "77.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.41,
      "mu": 1.67,
      "PhiF_H2O": 0.19,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77990",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N263A",
      "MUTATION_PDB": "N37A",
      "SEC_STR": "Coil",
      "RSA": "54.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.98,
      "mu": 1.55,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77991",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "N263A",
      "MUTATION_PDB": "N37A",
      "SEC_STR": "Coil",
      "RSA": "54.1",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.98,
      "mu": 1.55,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77991",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V265A",
      "MUTATION_PDB": "V39A",
      "SEC_STR": "Coil",
      "RSA": "7.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.03,
      "mu": 1.42,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77992",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V265A",
      "MUTATION_PDB": "V39A",
      "SEC_STR": "Coil",
      "RSA": "7.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.03,
      "mu": 1.42,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77992",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G267A",
      "MUTATION_PDB": "G41A",
      "SEC_STR": "Coil",
      "RSA": "22.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.23,
      "mu": 1.84,
      "PhiF_H2O": -0.02,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77993",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "G267A",
      "MUTATION_PDB": "G41A",
      "SEC_STR": "Coil",
      "RSA": "22.6",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.23,
      "mu": 1.84,
      "PhiF_H2O": -0.02,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77993",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y271L",
      "MUTATION_PDB": "Y45L",
      "SEC_STR": "Beta",
      "RSA": "36.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.89,
      "mu": 2.22,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77994",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "Y271L",
      "MUTATION_PDB": "Y45L",
      "SEC_STR": "Beta",
      "RSA": "36.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.89,
      "mu": 2.22,
      "PhiF_H2O": 0.3,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77994",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D272A",
      "MUTATION_PDB": "D46A",
      "SEC_STR": "Beta",
      "RSA": "49.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.88,
      "mu": 1.46,
      "PhiF_H2O": 0.96,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77995",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D272A",
      "MUTATION_PDB": "D46A",
      "SEC_STR": "Beta",
      "RSA": "49.7",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.88,
      "mu": 1.46,
      "PhiF_H2O": 0.96,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77995",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D273A",
      "MUTATION_PDB": "D47A",
      "SEC_STR": "Coil",
      "RSA": "55.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.26,
      "mu": 1.26,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77996",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "D273A",
      "MUTATION_PDB": "D47A",
      "SEC_STR": "Coil",
      "RSA": "55.8",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -6.26,
      "mu": 1.26,
      "PhiF_H2O": 0.67,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77996",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T275A",
      "MUTATION_PDB": "T49A",
      "SEC_STR": "Coil",
      "RSA": "58.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.32,
      "mu": 1.59,
      "PhiF_H2O": 0.84,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77997",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T275A",
      "MUTATION_PDB": "T49A",
      "SEC_STR": "Coil",
      "RSA": "58.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.32,
      "mu": 1.59,
      "PhiF_H2O": 0.84,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77997",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T277A",
      "MUTATION_PDB": "T51A",
      "SEC_STR": "Beta",
      "RSA": "15.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.99,
      "mu": 1.55,
      "PhiF_H2O": 0.44,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77998",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T277A",
      "MUTATION_PDB": "T51A",
      "SEC_STR": "Beta",
      "RSA": "15.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.99,
      "mu": 1.55,
      "PhiF_H2O": 0.44,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77998",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F278L",
      "MUTATION_PDB": "F52L",
      "SEC_STR": "Beta",
      "RSA": "2.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": 1.73,
      "mu": -9.67,
      "PhiF_H2O": 0.19,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77999",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "F278L",
      "MUTATION_PDB": "F52L",
      "SEC_STR": "Beta",
      "RSA": "2.5",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": 1.73,
      "mu": -9.67,
      "PhiF_H2O": 0.19,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/77999",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T279A",
      "MUTATION_PDB": "T53A",
      "SEC_STR": "Beta",
      "RSA": "23.2",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.18,
      "mu": 2.01,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/78000",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "T279A",
      "MUTATION_PDB": "T53A",
      "SEC_STR": "Beta",
      "RSA": "23.2",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -8.18,
      "mu": 2.01,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/78000",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V280A",
      "MUTATION_PDB": "V54A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.94,
      "mu": 2.8,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/78001",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Protein G",
      "SOURCE": "Streptococcus sp. GX7805",
      "LENGTH": 56.0,
      "UniProt": "P06654",
      "PDB_wild": "1pgb",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF01378"
      ],
      "CATH": [
         "1pgbA00 (3.10.20.10)"
      ],
      "MUTATION_UNIPROT": "V280A",
      "MUTATION_PDB": "V54A",
      "SEC_STR": "Beta",
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      "T": 22.0,
      "pH": 6.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "mf": -7.94,
      "mu": 2.8,
      "PhiF_H2O": 0.16,
      "AUTHOR_KIN": "McCallister, E.L., Alm, E., Baker, D.",
      "REFERENCE_KIN": "Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7, 669\u2013673. https://doi.org/10.1038/78001",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "10932252",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.63,
      "ln(ku)_H2O": -0.73,
      "dGKIN_H2O": 18.41,
      "mf": -2.93,
      "mu": 1.21,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2158",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.63,
      "ln(ku)_H2O": -0.73,
      "dGKIN_H2O": 18.41,
      "mf": -2.93,
      "mu": 1.21,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2158",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "V27A",
      "MUTATION_PDB": "V12A",
      "SEC_STR": "Beta",
      "RSA": "6.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.89,
      "dln(kf)_H2O": -0.74,
      "ln(ku)_H2O": 1.49,
      "dln(ku)_H2O": 2.22,
      "dGKIN_H2O": 10.88,
      "mf": -3.64,
      "mu": 0.92,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2159",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "V27A",
      "MUTATION_PDB": "V12A",
      "SEC_STR": "Beta",
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      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.89,
      "dln(kf)_H2O": -0.74,
      "ln(ku)_H2O": 1.49,
      "dln(ku)_H2O": 2.22,
      "dGKIN_H2O": 10.88,
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      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2159",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "E29A",
      "MUTATION_PDB": "E14A",
      "SEC_STR": "Beta",
      "RSA": "23.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.46,
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      "ln(ku)_H2O": -0.29,
      "dln(ku)_H2O": 0.44,
      "dGKIN_H2O": 16.74,
      "mf": -2.89,
      "mu": 1.26,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2160",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "E29A",
      "MUTATION_PDB": "E14A",
      "SEC_STR": "Beta",
      "RSA": "23.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.46,
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      "dln(ku)_H2O": 0.44,
      "dGKIN_H2O": 16.74,
      "mf": -2.89,
      "mu": 1.26,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2160",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "ADAh2",
      "SOURCE": "Homo sapiens",
      "LENGTH": 81.0,
      "UniProt": "P48052",
      "PDB_wild": "1o6x",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02244"
      ],
      "CATH": [
         "1o6xA00 (3.30.70.340)"
      ],
      "EC_NUMBER": "3.4.17.15",
      "MUTATION_UNIPROT": "I30V",
      "MUTATION_PDB": "I15V",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Phosphate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.78,
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      "ln(ku)_H2O": -0.87,
      "dln(ku)_H2O": -0.14,
      "dGKIN_H2O": 16.32,
      "mf": -2.8,
      "mu": 1.26,
      "PhiF_H2O": 1.0,
      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2161",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9799641",
      "STATE": "2",
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      "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.",
      "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283, 1027\u20131036. https://doi.org/10.1006/jmbi.1998.2175",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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         "1o6xA00 (3.30.70.340)"
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "Im9*",
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      "UniProt": "P13479",
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         "1imqA00 (1.10.1200.20)"
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      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.72,
      "ln(ku)_H2O": -3.0,
      "dGKIN_H2O": 26.56,
      "mf": -3.02,
      "mu": 1.02,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.079",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.72,
      "ln(ku)_H2O": -3.0,
      "dGKIN_H2O": 26.56,
      "mf": -3.02,
      "mu": 1.02,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.079",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "N56M",
      "MUTATION_PDB": "N56M",
      "SEC_STR": "Coil",
      "RSA": "43.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 9.3,
      "dln(kf)_H2O": 1.58,
      "ln(ku)_H2O": -1.97,
      "dln(ku)_H2O": 1.03,
      "dGKIN_H2O": 27.9,
      "ddGKIN_H2O": 1.34,
      "mf": -3.47,
      "mu": 0.94,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.080",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "N56M",
      "MUTATION_PDB": "N56M",
      "SEC_STR": "Coil",
      "RSA": "43.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 9.3,
      "dln(kf)_H2O": 1.58,
      "ln(ku)_H2O": -1.97,
      "dln(ku)_H2O": 1.03,
      "dGKIN_H2O": 27.9,
      "ddGKIN_H2O": 1.34,
      "mf": -3.47,
      "mu": 0.94,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.080",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "I58A",
      "MUTATION_PDB": "I58A",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.72,
      "dln(kf)_H2O": -3.0,
      "ln(ku)_H2O": -0.31,
      "dln(ku)_H2O": 2.69,
      "dGKIN_H2O": 12.47,
      "ddGKIN_H2O": -14.09,
      "mf": -2.87,
      "mu": 0.94,
      "PhiF_H2O": 0.6,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.081",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "I58A",
      "MUTATION_PDB": "I58A",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.72,
      "dln(kf)_H2O": -3.0,
      "ln(ku)_H2O": -0.31,
      "dln(ku)_H2O": 2.69,
      "dGKIN_H2O": 12.47,
      "ddGKIN_H2O": -14.09,
      "mf": -2.87,
      "mu": 0.94,
      "PhiF_H2O": 0.6,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.081",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "I58L",
      "MUTATION_PDB": "I58L",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.17,
      "dln(kf)_H2O": -0.55,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.47,
      "dGKIN_H2O": 24.02,
      "ddGKIN_H2O": -2.54,
      "mf": -3.07,
      "mu": 1.07,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.082",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "I58L",
      "MUTATION_PDB": "I58L",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.17,
      "dln(kf)_H2O": -0.55,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.47,
      "dGKIN_H2O": 24.02,
      "ddGKIN_H2O": -2.54,
      "mf": -3.07,
      "mu": 1.07,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.082",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "I58F",
      "MUTATION_PDB": "I58F",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.67,
      "dln(kf)_H2O": -0.05,
      "ln(ku)_H2O": -0.87,
      "dln(ku)_H2O": 2.13,
      "dGKIN_H2O": 21.16,
      "ddGKIN_H2O": -5.4,
      "mf": -3.47,
      "mu": 0.87,
      "PhiF_H2O": 0.03,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.083",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "I58F",
      "MUTATION_PDB": "I58F",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.67,
      "dln(kf)_H2O": -0.05,
      "ln(ku)_H2O": -0.87,
      "dln(ku)_H2O": 2.13,
      "dGKIN_H2O": 21.16,
      "ddGKIN_H2O": -5.4,
      "mf": -3.47,
      "mu": 0.87,
      "PhiF_H2O": 0.03,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.083",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "R59A",
      "MUTATION_PDB": "R59A",
      "SEC_STR": "Beta",
      "RSA": "34.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.69,
      "dln(kf)_H2O": 0.97,
      "ln(ku)_H2O": -2.41,
      "dln(ku)_H2O": 0.59,
      "dGKIN_H2O": 27.5,
      "ddGKIN_H2O": 0.94,
      "mf": -3.05,
      "mu": 0.97,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.084",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "R59A",
      "MUTATION_PDB": "R59A",
      "SEC_STR": "Beta",
      "RSA": "34.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.69,
      "dln(kf)_H2O": 0.97,
      "ln(ku)_H2O": -2.41,
      "dln(ku)_H2O": 0.59,
      "dGKIN_H2O": 27.5,
      "ddGKIN_H2O": 0.94,
      "mf": -3.05,
      "mu": 0.97,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.084",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V60A",
      "MUTATION_PDB": "V60A",
      "SEC_STR": "Beta",
      "RSA": "1.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.96,
      "dln(kf)_H2O": -2.76,
      "ln(ku)_H2O": -2.04,
      "dln(ku)_H2O": 0.96,
      "dGKIN_H2O": 17.33,
      "ddGKIN_H2O": -9.23,
      "mf": -3.2,
      "mu": 0.92,
      "PhiF_H2O": 0.63,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.085",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V60A",
      "MUTATION_PDB": "V60A",
      "SEC_STR": "Beta",
      "RSA": "1.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.96,
      "dln(kf)_H2O": -2.76,
      "ln(ku)_H2O": -2.04,
      "dln(ku)_H2O": 0.96,
      "dGKIN_H2O": 17.33,
      "ddGKIN_H2O": -9.23,
      "mf": -3.2,
      "mu": 0.92,
      "PhiF_H2O": 0.63,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.085",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L62A",
      "MUTATION_PDB": "L62A",
      "SEC_STR": "Coil",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.32,
      "dln(kf)_H2O": -2.4,
      "ln(ku)_H2O": 1.3,
      "dln(ku)_H2O": 4.3,
      "dGKIN_H2O": 9.96,
      "ddGKIN_H2O": -16.6,
      "mf": -3.2,
      "mu": 0.67,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.086",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L62A",
      "MUTATION_PDB": "L62A",
      "SEC_STR": "Coil",
      "RSA": "1.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.32,
      "dln(kf)_H2O": -2.4,
      "ln(ku)_H2O": 1.3,
      "dln(ku)_H2O": 4.3,
      "dGKIN_H2O": 9.96,
      "ddGKIN_H2O": -16.6,
      "mf": -3.2,
      "mu": 0.67,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.086",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "P63A",
      "MUTATION_PDB": "P63A",
      "SEC_STR": "Coil",
      "RSA": "33.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.34,
      "dln(kf)_H2O": -1.38,
      "ln(ku)_H2O": 0.54,
      "dln(ku)_H2O": 3.54,
      "dGKIN_H2O": 14.37,
      "ddGKIN_H2O": -12.19,
      "mf": -2.82,
      "mu": 0.72,
      "PhiF_H2O": 0.5,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.087",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "P63A",
      "MUTATION_PDB": "P63A",
      "SEC_STR": "Coil",
      "RSA": "33.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.34,
      "dln(kf)_H2O": -1.38,
      "ln(ku)_H2O": 0.54,
      "dln(ku)_H2O": 3.54,
      "dGKIN_H2O": 14.37,
      "ddGKIN_H2O": -12.19,
      "mf": -2.82,
      "mu": 0.72,
      "PhiF_H2O": 0.5,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.087",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "N64A",
      "MUTATION_PDB": "N64A",
      "SEC_STR": "Coil",
      "RSA": "59.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.56,
      "dln(kf)_H2O": -2.16,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 21.75,
      "ddGKIN_H2O": -4.81,
      "mf": -3.0,
      "mu": 1.09,
      "PhiF_H2O": 1.3,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.088",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "N64A",
      "MUTATION_PDB": "N64A",
      "SEC_STR": "Coil",
      "RSA": "59.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.56,
      "dln(kf)_H2O": -2.16,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 21.75,
      "ddGKIN_H2O": -4.81,
      "mf": -3.0,
      "mu": 1.09,
      "PhiF_H2O": 1.3,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.088",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "Q66A",
      "MUTATION_PDB": "Q66A",
      "SEC_STR": "Coil",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.38,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": -2.81,
      "dln(ku)_H2O": 0.19,
      "dGKIN_H2O": 25.25,
      "ddGKIN_H2O": -1.31,
      "mf": -3.22,
      "mu": 0.99,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.089",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "Q66A",
      "MUTATION_PDB": "Q66A",
      "SEC_STR": "Coil",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.38,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": -2.81,
      "dln(ku)_H2O": 0.19,
      "dGKIN_H2O": 25.25,
      "ddGKIN_H2O": -1.31,
      "mf": -3.22,
      "mu": 0.99,
      "PhiF_H2O": 0.35,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.089",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "T68A",
      "MUTATION_PDB": "T68A",
      "SEC_STR": "Coil",
      "RSA": "31.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.26,
      "dln(kf)_H2O": 0.54,
      "ln(ku)_H2O": -3.0,
      "dGKIN_H2O": 27.88,
      "ddGKIN_H2O": 1.32,
      "mf": -3.15,
      "mu": 1.16,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.090",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "T68A",
      "MUTATION_PDB": "T68A",
      "SEC_STR": "Coil",
      "RSA": "31.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.26,
      "dln(kf)_H2O": 0.54,
      "ln(ku)_H2O": -3.0,
      "dGKIN_H2O": 27.88,
      "ddGKIN_H2O": 1.32,
      "mf": -3.15,
      "mu": 1.16,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.090",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V69A",
      "MUTATION_PDB": "V69A",
      "SEC_STR": "Beta",
      "RSA": "59.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.52,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -2.41,
      "dln(ku)_H2O": 0.59,
      "dGKIN_H2O": 22.12,
      "ddGKIN_H2O": -4.44,
      "mf": -3.05,
      "mu": 1.02,
      "PhiF_H2O": 0.72,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.091",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V69A",
      "MUTATION_PDB": "V69A",
      "SEC_STR": "Beta",
      "RSA": "59.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.52,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -2.41,
      "dln(ku)_H2O": 0.59,
      "dGKIN_H2O": 22.12,
      "ddGKIN_H2O": -4.44,
      "mf": -3.05,
      "mu": 1.02,
      "PhiF_H2O": 0.72,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.091",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V70A",
      "MUTATION_PDB": "V70A",
      "SEC_STR": "Beta",
      "RSA": "13.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.28,
      "dln(kf)_H2O": -2.44,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.47,
      "dGKIN_H2O": 19.35,
      "ddGKIN_H2O": -7.21,
      "mf": -3.2,
      "mu": 0.89,
      "PhiF_H2O": 0.9,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.092",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V70A",
      "MUTATION_PDB": "V70A",
      "SEC_STR": "Beta",
      "RSA": "13.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.28,
      "dln(kf)_H2O": -2.44,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.47,
      "dGKIN_H2O": 19.35,
      "ddGKIN_H2O": -7.21,
      "mf": -3.2,
      "mu": 0.89,
      "PhiF_H2O": 0.9,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.092",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V72A",
      "MUTATION_PDB": "V72A",
      "SEC_STR": "Coil",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.52,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -2.81,
      "dln(ku)_H2O": 0.19,
      "dGKIN_H2O": 23.12,
      "ddGKIN_H2O": -3.44,
      "mf": -3.3,
      "mu": 0.99,
      "PhiF_H2O": 1.01,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.093",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V72A",
      "MUTATION_PDB": "V72A",
      "SEC_STR": "Coil",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.52,
      "dln(kf)_H2O": -1.2,
      "ln(ku)_H2O": -2.81,
      "dln(ku)_H2O": 0.19,
      "dGKIN_H2O": 23.12,
      "ddGKIN_H2O": -3.44,
      "mf": -3.3,
      "mu": 0.99,
      "PhiF_H2O": 1.01,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.093",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V72I",
      "MUTATION_PDB": "V72I",
      "SEC_STR": "Coil",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.82,
      "dln(kf)_H2O": 1.1,
      "ln(ku)_H2O": -0.58,
      "dln(ku)_H2O": 2.42,
      "dGKIN_H2O": 23.3,
      "ddGKIN_H2O": -3.26,
      "mf": -3.74,
      "mu": 0.87,
      "PhiF_H2O": -0.84,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.094",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V72I",
      "MUTATION_PDB": "V72I",
      "SEC_STR": "Coil",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.82,
      "dln(kf)_H2O": 1.1,
      "ln(ku)_H2O": -0.58,
      "dln(ku)_H2O": 2.42,
      "dGKIN_H2O": 23.3,
      "ddGKIN_H2O": -3.26,
      "mf": -3.74,
      "mu": 0.87,
      "PhiF_H2O": -0.84,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.094",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "M76A",
      "MUTATION_PDB": "M76A",
      "SEC_STR": "Coil",
      "RSA": "23.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.97,
      "dln(kf)_H2O": -0.75,
      "ln(ku)_H2O": -2.21,
      "dln(ku)_H2O": 0.79,
      "dGKIN_H2O": 22.73,
      "ddGKIN_H2O": -3.83,
      "mf": -3.22,
      "mu": 1.04,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.095",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "M76A",
      "MUTATION_PDB": "M76A",
      "SEC_STR": "Coil",
      "RSA": "23.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.97,
      "dln(kf)_H2O": -0.75,
      "ln(ku)_H2O": -2.21,
      "dln(ku)_H2O": 0.79,
      "dGKIN_H2O": 22.73,
      "ddGKIN_H2O": -3.83,
      "mf": -3.22,
      "mu": 1.04,
      "PhiF_H2O": 0.25,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.095",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "S77A",
      "MUTATION_PDB": "S77A",
      "SEC_STR": "Coil",
      "RSA": "23.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.99,
      "dln(kf)_H2O": -1.73,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 0.7,
      "dGKIN_H2O": 20.56,
      "ddGKIN_H2O": -6.0,
      "mf": -3.02,
      "mu": 1.02,
      "PhiF_H2O": 0.72,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.096",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "S77A",
      "MUTATION_PDB": "S77A",
      "SEC_STR": "Coil",
      "RSA": "23.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.99,
      "dln(kf)_H2O": -1.73,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 0.7,
      "dGKIN_H2O": 20.56,
      "ddGKIN_H2O": -6.0,
      "mf": -3.02,
      "mu": 1.02,
      "PhiF_H2O": 0.72,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.096",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "S77T",
      "MUTATION_PDB": "S77T",
      "SEC_STR": "Coil",
      "RSA": "23.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.85,
      "dln(kf)_H2O": 0.13,
      "ln(ku)_H2O": -4.61,
      "dln(ku)_H2O": -1.61,
      "dGKIN_H2O": 30.85,
      "ddGKIN_H2O": 4.29,
      "mf": -2.97,
      "mu": 1.29,
      "PhiF_H2O": 0.09,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.097",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "S77T",
      "MUTATION_PDB": "S77T",
      "SEC_STR": "Coil",
      "RSA": "23.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.85,
      "dln(kf)_H2O": 0.13,
      "ln(ku)_H2O": -4.61,
      "dln(ku)_H2O": -1.61,
      "dGKIN_H2O": 30.85,
      "ddGKIN_H2O": 4.29,
      "mf": -2.97,
      "mu": 1.29,
      "PhiF_H2O": 0.09,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.097",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L78A",
      "MUTATION_PDB": "L78A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.99,
      "dln(kf)_H2O": -1.73,
      "ln(ku)_H2O": 1.8,
      "dln(ku)_H2O": 4.8,
      "dGKIN_H2O": 10.38,
      "ddGKIN_H2O": -16.18,
      "mf": -3.12,
      "mu": 0.97,
      "PhiF_H2O": 0.29,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.098",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L78A",
      "MUTATION_PDB": "L78A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.99,
      "dln(kf)_H2O": -1.73,
      "ln(ku)_H2O": 1.8,
      "dln(ku)_H2O": 4.8,
      "dGKIN_H2O": 10.38,
      "ddGKIN_H2O": -16.18,
      "mf": -3.12,
      "mu": 0.97,
      "PhiF_H2O": 0.29,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.098",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "D80A",
      "MUTATION_PDB": "D80A",
      "SEC_STR": "Helix",
      "RSA": "54.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.81,
      "dln(kf)_H2O": -0.91,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 24.85,
      "ddGKIN_H2O": -1.71,
      "mf": -2.92,
      "mu": 1.07,
      "PhiF_H2O": 0.56,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.099",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "D80A",
      "MUTATION_PDB": "D80A",
      "SEC_STR": "Helix",
      "RSA": "54.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.81,
      "dln(kf)_H2O": -0.91,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 24.85,
      "ddGKIN_H2O": -1.71,
      "mf": -2.92,
      "mu": 1.07,
      "PhiF_H2O": 0.56,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.099",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C81A",
      "MUTATION_PDB": "C81A",
      "SEC_STR": "Helix",
      "RSA": "2.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.81,
      "dln(kf)_H2O": 0.09,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 27.33,
      "ddGKIN_H2O": 0.77,
      "mf": -2.9,
      "mu": 1.04,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.100",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C81A",
      "MUTATION_PDB": "C81A",
      "SEC_STR": "Helix",
      "RSA": "2.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.81,
      "dln(kf)_H2O": 0.09,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 27.33,
      "ddGKIN_H2O": 0.77,
      "mf": -2.9,
      "mu": 1.04,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.100",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C81I",
      "MUTATION_PDB": "C81I",
      "SEC_STR": "Helix",
      "RSA": "2.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 10.12,
      "dln(kf)_H2O": 2.4,
      "ln(ku)_H2O": -0.78,
      "dln(ku)_H2O": 2.22,
      "dGKIN_H2O": 27.0,
      "ddGKIN_H2O": 0.44,
      "mf": -3.77,
      "mu": 0.94,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.101",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C81I",
      "MUTATION_PDB": "C81I",
      "SEC_STR": "Helix",
      "RSA": "2.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 10.12,
      "dln(kf)_H2O": 2.4,
      "ln(ku)_H2O": -0.78,
      "dln(ku)_H2O": 2.22,
      "dGKIN_H2O": 27.0,
      "ddGKIN_H2O": 0.44,
      "mf": -3.77,
      "mu": 0.94,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.101",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L82A",
      "MUTATION_PDB": "L82A",
      "SEC_STR": "Helix",
      "RSA": "3.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.12,
      "dln(kf)_H2O": -1.6,
      "ln(ku)_H2O": -0.16,
      "dln(ku)_H2O": 2.84,
      "dGKIN_H2O": 15.56,
      "ddGKIN_H2O": -11.0,
      "mf": -4.61,
      "mu": 1.14,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.102",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L82A",
      "MUTATION_PDB": "L82A",
      "SEC_STR": "Helix",
      "RSA": "3.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.12,
      "dln(kf)_H2O": -1.6,
      "ln(ku)_H2O": -0.16,
      "dln(ku)_H2O": 2.84,
      "dGKIN_H2O": 15.56,
      "ddGKIN_H2O": -11.0,
      "mf": -4.61,
      "mu": 1.14,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.102",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A85G",
      "MUTATION_PDB": "A85G",
      "SEC_STR": "Helix",
      "RSA": "4.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.27,
      "dln(kf)_H2O": -1.45,
      "ln(ku)_H2O": -1.31,
      "dln(ku)_H2O": 1.69,
      "dGKIN_H2O": 18.79,
      "ddGKIN_H2O": -7.77,
      "mf": -3.67,
      "mu": 0.92,
      "PhiF_H2O": 0.56,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.103",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A85G",
      "MUTATION_PDB": "A85G",
      "SEC_STR": "Helix",
      "RSA": "4.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.27,
      "dln(kf)_H2O": -1.45,
      "ln(ku)_H2O": -1.31,
      "dln(ku)_H2O": 1.69,
      "dGKIN_H2O": 18.79,
      "ddGKIN_H2O": -7.77,
      "mf": -3.67,
      "mu": 0.92,
      "PhiF_H2O": 0.56,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.103",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L86A",
      "MUTATION_PDB": "L86A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.53,
      "dln(kf)_H2O": -2.19,
      "ln(ku)_H2O": 1.02,
      "dln(ku)_H2O": 4.02,
      "dGKIN_H2O": 11.17,
      "ddGKIN_H2O": -15.39,
      "mf": -3.17,
      "mu": 0.67,
      "PhiF_H2O": 0.44,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.104",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L86A",
      "MUTATION_PDB": "L86A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.53,
      "dln(kf)_H2O": -2.19,
      "ln(ku)_H2O": 1.02,
      "dln(ku)_H2O": 4.02,
      "dGKIN_H2O": 11.17,
      "ddGKIN_H2O": -15.39,
      "mf": -3.17,
      "mu": 0.67,
      "PhiF_H2O": 0.44,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.104",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "R89L",
      "MUTATION_PDB": "R89L",
      "SEC_STR": "Helix",
      "RSA": "33.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 10.33,
      "dln(kf)_H2O": 2.61,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 33.57,
      "ddGKIN_H2O": 7.01,
      "mf": -3.12,
      "mu": 1.14,
      "PhiF_H2O": 1.2,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.105",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "R89L",
      "MUTATION_PDB": "R89L",
      "SEC_STR": "Helix",
      "RSA": "33.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 10.33,
      "dln(kf)_H2O": 2.61,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 33.57,
      "ddGKIN_H2O": 7.01,
      "mf": -3.12,
      "mu": 1.14,
      "PhiF_H2O": 1.2,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.105",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L91A",
      "MUTATION_PDB": "L91A",
      "SEC_STR": "Coil",
      "RSA": "39.6",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.49,
      "dln(kf)_H2O": -0.23,
      "ln(ku)_H2O": -0.73,
      "dln(ku)_H2O": 2.27,
      "dGKIN_H2O": 20.38,
      "ddGKIN_H2O": -6.18,
      "mf": -3.72,
      "mu": 0.94,
      "PhiF_H2O": 0.1,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.106",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L91A",
      "MUTATION_PDB": "L91A",
      "SEC_STR": "Coil",
      "RSA": "39.6",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.49,
      "dln(kf)_H2O": -0.23,
      "ln(ku)_H2O": -0.73,
      "dln(ku)_H2O": 2.27,
      "dGKIN_H2O": 20.38,
      "ddGKIN_H2O": -6.18,
      "mf": -3.72,
      "mu": 0.94,
      "PhiF_H2O": 0.1,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.106",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "P93A",
      "MUTATION_PDB": "P93A",
      "SEC_STR": "Coil",
      "RSA": "2.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.22,
      "dln(kf)_H2O": 0.5,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 0.7,
      "dGKIN_H2O": 26.06,
      "ddGKIN_H2O": -0.5,
      "mf": -3.32,
      "mu": 0.92,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.107",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "P93A",
      "MUTATION_PDB": "P93A",
      "SEC_STR": "Coil",
      "RSA": "2.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.22,
      "dln(kf)_H2O": 0.5,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 0.7,
      "dGKIN_H2O": 26.06,
      "ddGKIN_H2O": -0.5,
      "mf": -3.32,
      "mu": 0.92,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.107",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C95A",
      "MUTATION_PDB": "C95A",
      "SEC_STR": "Coil",
      "RSA": "51.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.05,
      "dln(kf)_H2O": -0.67,
      "ln(ku)_H2O": -3.0,
      "dGKIN_H2O": 24.88,
      "ddGKIN_H2O": -1.68,
      "mf": -2.75,
      "mu": 1.07,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.108",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C95A",
      "MUTATION_PDB": "C95A",
      "SEC_STR": "Coil",
      "RSA": "51.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.05,
      "dln(kf)_H2O": -0.67,
      "ln(ku)_H2O": -3.0,
      "dGKIN_H2O": 24.88,
      "ddGKIN_H2O": -1.68,
      "mf": -2.75,
      "mu": 1.07,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.108",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C96A",
      "MUTATION_PDB": "C96A",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.15,
      "dln(kf)_H2O": 0.43,
      "ln(ku)_H2O": -0.11,
      "dln(ku)_H2O": 2.89,
      "dGKIN_H2O": 20.44,
      "ddGKIN_H2O": -6.12,
      "mf": -3.22,
      "mu": 0.89,
      "PhiF_H2O": -0.1,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.109",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C96A",
      "MUTATION_PDB": "C96A",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.15,
      "dln(kf)_H2O": 0.43,
      "ln(ku)_H2O": -0.11,
      "dln(ku)_H2O": 2.89,
      "dGKIN_H2O": 20.44,
      "ddGKIN_H2O": -6.12,
      "mf": -3.22,
      "mu": 0.89,
      "PhiF_H2O": -0.1,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.109",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C96L",
      "MUTATION_PDB": "C96L",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.36,
      "dln(kf)_H2O": -0.36,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 26.22,
      "ddGKIN_H2O": -0.34,
      "mf": -2.73,
      "mu": 1.21,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.110",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C96L",
      "MUTATION_PDB": "C96L",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.36,
      "dln(kf)_H2O": -0.36,
      "ln(ku)_H2O": -3.22,
      "dln(ku)_H2O": -0.22,
      "dGKIN_H2O": 26.22,
      "ddGKIN_H2O": -0.34,
      "mf": -2.73,
      "mu": 1.21,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.110",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C96M",
      "MUTATION_PDB": "C96M",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.9,
      "dln(kf)_H2O": 0.18,
      "ln(ku)_H2O": -3.51,
      "dln(ku)_H2O": -0.51,
      "dGKIN_H2O": 28.26,
      "ddGKIN_H2O": 1.7,
      "mf": -3.1,
      "mu": 1.16,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.111",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "C96M",
      "MUTATION_PDB": "C96M",
      "SEC_STR": "Beta",
      "RSA": "14.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.9,
      "dln(kf)_H2O": 0.18,
      "ln(ku)_H2O": -3.51,
      "dln(ku)_H2O": -0.51,
      "dGKIN_H2O": 28.26,
      "ddGKIN_H2O": 1.7,
      "mf": -3.1,
      "mu": 1.16,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.111",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A97G",
      "MUTATION_PDB": "A97G",
      "SEC_STR": "Beta",
      "RSA": "0.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.05,
      "dln(kf)_H2O": -0.67,
      "ln(ku)_H2O": -1.56,
      "dln(ku)_H2O": 1.44,
      "dGKIN_H2O": 21.33,
      "ddGKIN_H2O": -5.23,
      "mf": -2.9,
      "mu": 0.92,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.112",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A97G",
      "MUTATION_PDB": "A97G",
      "SEC_STR": "Beta",
      "RSA": "0.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.05,
      "dln(kf)_H2O": -0.67,
      "ln(ku)_H2O": -1.56,
      "dln(ku)_H2O": 1.44,
      "dGKIN_H2O": 21.33,
      "ddGKIN_H2O": -5.23,
      "mf": -2.9,
      "mu": 0.92,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.112",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V98A",
      "MUTATION_PDB": "V98A",
      "SEC_STR": "Beta",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.73,
      "dln(kf)_H2O": -1.99,
      "ln(ku)_H2O": -1.24,
      "dln(ku)_H2O": 1.76,
      "dGKIN_H2O": 17.26,
      "ddGKIN_H2O": -9.3,
      "mf": -2.28,
      "mu": 0.92,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.113",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V98A",
      "MUTATION_PDB": "V98A",
      "SEC_STR": "Beta",
      "RSA": "2.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.73,
      "dln(kf)_H2O": -1.99,
      "ln(ku)_H2O": -1.24,
      "dln(ku)_H2O": 1.76,
      "dGKIN_H2O": 17.26,
      "ddGKIN_H2O": -9.3,
      "mf": -2.28,
      "mu": 0.92,
      "PhiF_H2O": 0.48,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.113",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "R100A",
      "MUTATION_PDB": "R100A",
      "SEC_STR": "Beta",
      "RSA": "10.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.5,
      "dln(kf)_H2O": -0.22,
      "ln(ku)_H2O": -1.61,
      "dln(ku)_H2O": 1.39,
      "dGKIN_H2O": 22.57,
      "ddGKIN_H2O": -3.99,
      "mf": -2.95,
      "mu": 0.97,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.114",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "R100A",
      "MUTATION_PDB": "R100A",
      "SEC_STR": "Beta",
      "RSA": "10.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.5,
      "dln(kf)_H2O": -0.22,
      "ln(ku)_H2O": -1.61,
      "dln(ku)_H2O": 1.39,
      "dGKIN_H2O": 22.57,
      "ddGKIN_H2O": -3.99,
      "mf": -2.95,
      "mu": 0.97,
      "PhiF_H2O": 0.21,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.114",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "E104A",
      "MUTATION_PDB": "E104A",
      "SEC_STR": "Coil",
      "RSA": "61.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.08,
      "dln(kf)_H2O": 0.36,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.47,
      "dGKIN_H2O": 26.28,
      "ddGKIN_H2O": -0.28,
      "mf": -3.2,
      "mu": 0.92,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.115",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "E104A",
      "MUTATION_PDB": "E104A",
      "SEC_STR": "Coil",
      "RSA": "61.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.08,
      "dln(kf)_H2O": 0.36,
      "ln(ku)_H2O": -2.53,
      "dln(ku)_H2O": 0.47,
      "dGKIN_H2O": 26.28,
      "ddGKIN_H2O": -0.28,
      "mf": -3.2,
      "mu": 0.92,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.115",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "K109A",
      "MUTATION_PDB": "K109A",
      "SEC_STR": "Coil",
      "RSA": "22.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.01,
      "dln(kf)_H2O": 0.29,
      "ln(ku)_H2O": -1.66,
      "dln(ku)_H2O": 1.34,
      "dGKIN_H2O": 23.97,
      "ddGKIN_H2O": -2.59,
      "mf": -3.25,
      "mu": 0.84,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.116",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "K109A",
      "MUTATION_PDB": "K109A",
      "SEC_STR": "Coil",
      "RSA": "22.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.01,
      "dln(kf)_H2O": 0.29,
      "ln(ku)_H2O": -1.66,
      "dln(ku)_H2O": 1.34,
      "dGKIN_H2O": 23.97,
      "ddGKIN_H2O": -2.59,
      "mf": -3.25,
      "mu": 0.84,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.116",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L112A",
      "MUTATION_PDB": "L112A",
      "SEC_STR": "Coil",
      "RSA": "15.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.07,
      "dln(kf)_H2O": -1.65,
      "ln(ku)_H2O": 1.01,
      "dln(ku)_H2O": 4.01,
      "dGKIN_H2O": 12.54,
      "ddGKIN_H2O": -14.02,
      "mf": -2.48,
      "mu": 0.89,
      "PhiF_H2O": 0.41,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.117",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L112A",
      "MUTATION_PDB": "L112A",
      "SEC_STR": "Coil",
      "RSA": "15.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.07,
      "dln(kf)_H2O": -1.65,
      "ln(ku)_H2O": 1.01,
      "dln(ku)_H2O": 4.01,
      "dGKIN_H2O": 12.54,
      "ddGKIN_H2O": -14.02,
      "mf": -2.48,
      "mu": 0.89,
      "PhiF_H2O": 0.41,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.117",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "D117A",
      "MUTATION_PDB": "D117A",
      "SEC_STR": "Coil",
      "RSA": "55.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.38,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 0.7,
      "dGKIN_H2O": 23.98,
      "ddGKIN_H2O": -2.58,
      "mf": -3.12,
      "mu": 1.02,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.118",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "D117A",
      "MUTATION_PDB": "D117A",
      "SEC_STR": "Coil",
      "RSA": "55.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.38,
      "dln(kf)_H2O": -0.34,
      "ln(ku)_H2O": -2.3,
      "dln(ku)_H2O": 0.7,
      "dGKIN_H2O": 23.98,
      "ddGKIN_H2O": -2.58,
      "mf": -3.12,
      "mu": 1.02,
      "PhiF_H2O": 0.2,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.118",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A118G",
      "MUTATION_PDB": "A118G",
      "SEC_STR": "Helix",
      "RSA": "1.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.51,
      "dln(kf)_H2O": -1.21,
      "ln(ku)_H2O": -0.73,
      "dln(ku)_H2O": 2.27,
      "dGKIN_H2O": 17.94,
      "ddGKIN_H2O": -8.62,
      "mf": -2.6,
      "mu": 1.14,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.119",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A118G",
      "MUTATION_PDB": "A118G",
      "SEC_STR": "Helix",
      "RSA": "1.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.51,
      "dln(kf)_H2O": -1.21,
      "ln(ku)_H2O": -0.73,
      "dln(ku)_H2O": 2.27,
      "dGKIN_H2O": 17.94,
      "ddGKIN_H2O": -8.62,
      "mf": -2.6,
      "mu": 1.14,
      "PhiF_H2O": 0.39,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.119",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A118L",
      "MUTATION_PDB": "A118L",
      "SEC_STR": "Helix",
      "RSA": "1.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.28,
      "dln(kf)_H2O": -0.44,
      "ln(ku)_H2O": 1.17,
      "dln(ku)_H2O": 4.17,
      "dGKIN_H2O": 15.14,
      "ddGKIN_H2O": -11.42,
      "mf": -2.85,
      "mu": 0.77,
      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.120",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "A118L",
      "MUTATION_PDB": "A118L",
      "SEC_STR": "Helix",
      "RSA": "1.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.28,
      "dln(kf)_H2O": -0.44,
      "ln(ku)_H2O": 1.17,
      "dln(ku)_H2O": 4.17,
      "dGKIN_H2O": 15.14,
      "ddGKIN_H2O": -11.42,
      "mf": -2.85,
      "mu": 0.77,
      "PhiF_H2O": 0.11,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.120",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L121A",
      "MUTATION_PDB": "L121A",
      "SEC_STR": "Coil",
      "RSA": "9.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.73,
      "dln(kf)_H2O": -0.99,
      "ln(ku)_H2O": 0.67,
      "dln(ku)_H2O": 3.67,
      "dGKIN_H2O": 14.99,
      "ddGKIN_H2O": -11.57,
      "mf": -2.82,
      "mu": 0.99,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.121",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L121A",
      "MUTATION_PDB": "L121A",
      "SEC_STR": "Coil",
      "RSA": "9.1",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.73,
      "dln(kf)_H2O": -0.99,
      "ln(ku)_H2O": 0.67,
      "dln(ku)_H2O": 3.67,
      "dGKIN_H2O": 14.99,
      "ddGKIN_H2O": -11.57,
      "mf": -2.82,
      "mu": 0.99,
      "PhiF_H2O": 0.26,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.121",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "E124A",
      "MUTATION_PDB": "E124A",
      "SEC_STR": "Coil",
      "RSA": "22.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.55,
      "dln(kf)_H2O": -0.17,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": 0.34,
      "dGKIN_H2O": 25.31,
      "ddGKIN_H2O": -1.25,
      "mf": -3.0,
      "mu": 0.99,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.122",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "E124A",
      "MUTATION_PDB": "E124A",
      "SEC_STR": "Coil",
      "RSA": "22.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.55,
      "dln(kf)_H2O": -0.17,
      "ln(ku)_H2O": -2.66,
      "dln(ku)_H2O": 0.34,
      "dGKIN_H2O": 25.31,
      "ddGKIN_H2O": -1.25,
      "mf": -3.0,
      "mu": 0.99,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.122",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "E125A",
      "MUTATION_PDB": "E125A",
      "SEC_STR": "Beta",
      "RSA": "24.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.91,
      "dln(kf)_H2O": -0.81,
      "ln(ku)_H2O": -2.81,
      "dln(ku)_H2O": 0.19,
      "dGKIN_H2O": 24.09,
      "ddGKIN_H2O": -2.47,
      "mf": -3.0,
      "mu": 1.07,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.123",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "E125A",
      "MUTATION_PDB": "E125A",
      "SEC_STR": "Beta",
      "RSA": "24.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.91,
      "dln(kf)_H2O": -0.81,
      "ln(ku)_H2O": -2.81,
      "dln(ku)_H2O": 0.19,
      "dGKIN_H2O": 24.09,
      "ddGKIN_H2O": -2.47,
      "mf": -3.0,
      "mu": 1.07,
      "PhiF_H2O": 0.86,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.123",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L126A",
      "MUTATION_PDB": "L126A",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.34,
      "dln(kf)_H2O": -2.38,
      "ln(ku)_H2O": 0.83,
      "dln(ku)_H2O": 3.83,
      "dGKIN_H2O": 11.16,
      "ddGKIN_H2O": -15.4,
      "mf": -3.32,
      "mu": 0.79,
      "PhiF_H2O": 0.45,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.124",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "L126A",
      "MUTATION_PDB": "L126A",
      "SEC_STR": "Beta",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.34,
      "dln(kf)_H2O": -2.38,
      "ln(ku)_H2O": 0.83,
      "dln(ku)_H2O": 3.83,
      "dGKIN_H2O": 11.16,
      "ddGKIN_H2O": -15.4,
      "mf": -3.32,
      "mu": 0.79,
      "PhiF_H2O": 0.45,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.124",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V128A",
      "MUTATION_PDB": "V128A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.5,
      "dln(kf)_H2O": -2.22,
      "ln(ku)_H2O": 1.16,
      "dln(ku)_H2O": 4.16,
      "dGKIN_H2O": 10.74,
      "ddGKIN_H2O": -15.82,
      "mf": -3.0,
      "mu": 0.82,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.125",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "V128A",
      "MUTATION_PDB": "V128A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.5,
      "dln(kf)_H2O": -2.22,
      "ln(ku)_H2O": 1.16,
      "dln(ku)_H2O": 4.16,
      "dGKIN_H2O": 10.74,
      "ddGKIN_H2O": -15.82,
      "mf": -3.0,
      "mu": 0.82,
      "PhiF_H2O": 0.42,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.125",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "D129A",
      "MUTATION_PDB": "D129A",
      "SEC_STR": "Beta",
      "RSA": "20.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.43,
      "dln(kf)_H2O": -0.29,
      "ln(ku)_H2O": -2.41,
      "dln(ku)_H2O": 0.59,
      "dGKIN_H2O": 24.37,
      "ddGKIN_H2O": -2.19,
      "mf": -3.1,
      "mu": 1.14,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.126",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "raf RBD",
      "SOURCE": "Homo sapiens",
      "LENGTH": 79.0,
      "UniProt": "P04049",
      "PDB_wild": "1rfa",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02196"
      ],
      "CATH": [
         "1rfaA00 (3.10.20.90)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_UNIPROT": "D129A",
      "MUTATION_PDB": "D129A",
      "SEC_STR": "Beta",
      "RSA": "20.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 7.43,
      "dln(kf)_H2O": -0.29,
      "ln(ku)_H2O": -2.41,
      "dln(ku)_H2O": 0.59,
      "dGKIN_H2O": 24.37,
      "ddGKIN_H2O": -2.19,
      "mf": -3.1,
      "mu": 1.14,
      "PhiF_H2O": 0.38,
      "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.",
      "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.126",
      "YEAR_KIN": 2007.0,
      "PMID_KIN": "17137592",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Sso7d (Y34W)",
      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "E12A",
      "MUTATION_PDB": "E12A",
      "SEC_STR": "Beta",
      "RSA": "53.1",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.83,
      "dln(kf)_H2O": -0.12,
      "ln(ku)_H2O": -2.86,
      "dln(ku)_H2O": 0.38,
      "dGKIN_H2O": 23.6,
      "ddGKIN_H2O": -1.21,
      "mf": -4.82,
      "mu": 2.51,
      "PhiF_H2O": 0.24,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4236",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Sso7d (Y34W)",
      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "E12A",
      "MUTATION_PDB": "E12A",
      "SEC_STR": "Beta",
      "RSA": "53.1",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.83,
      "dln(kf)_H2O": -0.12,
      "ln(ku)_H2O": -2.86,
      "dln(ku)_H2O": 0.38,
      "dGKIN_H2O": 23.6,
      "ddGKIN_H2O": -1.21,
      "mf": -4.82,
      "mu": 2.51,
      "PhiF_H2O": 0.24,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4236",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Sso7d (Y34W)",
      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "V15A",
      "MUTATION_PDB": "V15A",
      "SEC_STR": "Beta",
      "RSA": "11.3",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.06,
      "dln(kf)_H2O": 0.11,
      "ln(ku)_H2O": 0.81,
      "dln(ku)_H2O": 4.05,
      "dGKIN_H2O": 15.23,
      "ddGKIN_H2O": -9.58,
      "mf": -5.07,
      "mu": 2.24,
      "PhiF_H2O": -0.03,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4237",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Sso7d (Y34W)",
      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "V15A",
      "MUTATION_PDB": "V15A",
      "SEC_STR": "Beta",
      "RSA": "11.3",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.06,
      "dln(kf)_H2O": 0.11,
      "ln(ku)_H2O": 0.81,
      "dln(ku)_H2O": 4.05,
      "dGKIN_H2O": 15.23,
      "ddGKIN_H2O": -9.58,
      "mf": -5.07,
      "mu": 2.24,
      "PhiF_H2O": -0.03,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4237",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Sso7d (Y34W)",
      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "I17A",
      "MUTATION_PDB": "I17A",
      "SEC_STR": "Helix",
      "RSA": "1.2",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.03,
      "dln(kf)_H2O": 0.08,
      "ln(ku)_H2O": -1.08,
      "dln(ku)_H2O": 2.16,
      "dGKIN_H2O": 19.75,
      "ddGKIN_H2O": -5.06,
      "mf": -4.56,
      "mu": 2.83,
      "PhiF_H2O": -0.04,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4238",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Sso7d (Y34W)",
      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "I17A",
      "MUTATION_PDB": "I17A",
      "SEC_STR": "Helix",
      "RSA": "1.2",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.03,
      "dln(kf)_H2O": 0.08,
      "ln(ku)_H2O": -1.08,
      "dln(ku)_H2O": 2.16,
      "dGKIN_H2O": 19.75,
      "ddGKIN_H2O": -5.06,
      "mf": -4.56,
      "mu": 2.83,
      "PhiF_H2O": -0.04,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4238",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "S18A",
      "MUTATION_PDB": "S18A",
      "SEC_STR": "Helix",
      "RSA": "60.0",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.95,
      "ln(ku)_H2O": -3.02,
      "dln(ku)_H2O": 0.22,
      "dGKIN_H2O": 24.27,
      "ddGKIN_H2O": -0.54,
      "PhiF_H2O": -0.02,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4239",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "S18A",
      "MUTATION_PDB": "S18A",
      "SEC_STR": "Helix",
      "RSA": "60.0",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.95,
      "ln(ku)_H2O": -3.02,
      "dln(ku)_H2O": 0.22,
      "dGKIN_H2O": 24.27,
      "ddGKIN_H2O": -0.54,
      "PhiF_H2O": -0.02,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
      ],
      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4239",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "V23A",
      "MUTATION_PDB": "V23A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 20.0,
      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.45,
      "dln(kf)_H2O": -0.5,
      "ln(ku)_H2O": -3.35,
      "dln(ku)_H2O": -0.11,
      "dGKIN_H2O": 23.85,
      "ddGKIN_H2O": -0.96,
      "mf": -4.6,
      "mu": 2.66,
      "PhiF_H2O": 1.27,
      "BACKGROUND_MUT_UNIPROT": [
         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
         "Y34W"
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      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4241",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02294"
      ],
      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "V23A",
      "MUTATION_PDB": "V23A",
      "SEC_STR": "Beta",
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      "pH": 6.1,
      "BUFFER_NAME": "MES",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.45,
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      "ln(ku)_H2O": -3.35,
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      "dGKIN_H2O": 23.85,
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         "Y34W"
      ],
      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4241",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
      "UniProt": "P39476",
      "PDB_wild": "1bnz",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1bnzA00 (2.40.50.40)"
      ],
      "MUTATION_UNIPROT": "R25A",
      "MUTATION_PDB": "R25A",
      "SEC_STR": "Beta",
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Guerois, R., Serrano, L.",
      "REFERENCE_KIN": "The SH3-fold family: experimental evidence and prediction of variations in the folding pathways. J. Mol. Biol. 304, 967\u2013982. https://doi.org/10.1006/jmbi.2000.4242",
      "YEAR_KIN": 2000.0,
      "PMID_KIN": "11124040",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Saccharolobus solfataricus",
      "LENGTH": 64.0,
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      "ln(kf)_H2O": 6.32,
      "ln(ku)_H2O": 2.3,
      "dGKIN_H2O": 11.13,
      "AUTHOR_KIN": "Perl, D., Welker, C., Schindler, T., Schr\u00f6der, K., Marahiel, M.A., Jaenicke, R., Schmid, F.X.",
      "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct. Biol. 5, 229\u2013235. https://doi.org/10.1038/nsb0398-229",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9501917",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.32,
      "ln(ku)_H2O": 2.3,
      "dGKIN_H2O": 11.13,
      "AUTHOR_KIN": "Perl, D., Welker, C., Schindler, T., Schr\u00f6der, K., Marahiel, M.A., Jaenicke, R., Schmid, F.X.",
      "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat. Struct. Biol. 5, 229\u2013235. https://doi.org/10.1038/nsb0398-229",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9501917",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "WT(E3L)",
      "MUTATION_PDB": "WT(E3L)",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.99,
      "ln(ku)_H2O": 0.47,
      "dGKIN_H2O": "15.6",
      "mf": -2.3,
      "mu": 0.32,
      "CM_KIN": 5.97,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.011",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "WT(E3L)",
      "MUTATION_PDB": "WT(E3L)",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.99,
      "ln(ku)_H2O": 0.47,
      "dGKIN_H2O": "15.6",
      "mf": -2.3,
      "mu": 0.32,
      "CM_KIN": 5.97,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.011",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "L2A",
      "MUTATION_PDB": "L2A",
      "SEC_STR": "Beta",
      "RSA": "37.2",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.87,
      "dln(kf)_H2O": -0.12,
      "ln(ku)_H2O": 0.57,
      "dln(ku)_H2O": 0.1,
      "dGKIN_H2O": "15.1",
      "mf": -2.3,
      "mu": 0.32,
      "CM_KIN": 5.76,
      "PhiF_H2O": -0.4,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.012",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "L2A",
      "MUTATION_PDB": "L2A",
      "SEC_STR": "Beta",
      "RSA": "37.2",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.87,
      "dln(kf)_H2O": -0.12,
      "ln(ku)_H2O": 0.57,
      "dln(ku)_H2O": 0.1,
      "dGKIN_H2O": "15.1",
      "mf": -2.3,
      "mu": 0.32,
      "CM_KIN": 5.76,
      "PhiF_H2O": -0.4,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.012",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "L3E",
      "MUTATION_PDB": "L3E",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.17,
      "dln(kf)_H2O": -0.82,
      "ln(ku)_H2O": 1.52,
      "dln(ku)_H2O": 1.05,
      "dGKIN_H2O": "11.1",
      "mf": -2.38,
      "mu": 0.32,
      "CM_KIN": 4.12,
      "PhiF_H2O": 0.44,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.013",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "L3E",
      "MUTATION_PDB": "L3E",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.17,
      "dln(kf)_H2O": -0.82,
      "ln(ku)_H2O": 1.52,
      "dln(ku)_H2O": 1.05,
      "dGKIN_H2O": "11.1",
      "mf": -2.38,
      "mu": 0.32,
      "CM_KIN": 4.12,
      "PhiF_H2O": 0.44,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
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      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.013",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "K5A",
      "MUTATION_PDB": "K5A",
      "SEC_STR": "Beta",
      "RSA": "49.3",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.1,
      "dln(kf)_H2O": -1.89,
      "ln(ku)_H2O": 1.02,
      "dln(ku)_H2O": 0.55,
      "dGKIN_H2O": "9.8",
      "mf": -2.81,
      "mu": 0.32,
      "CM_KIN": 3.12,
      "PhiF_H2O": 0.78,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.014",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "K5A",
      "MUTATION_PDB": "K5A",
      "SEC_STR": "Beta",
      "RSA": "49.3",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.1,
      "dln(kf)_H2O": -1.89,
      "ln(ku)_H2O": 1.02,
      "dln(ku)_H2O": 0.55,
      "dGKIN_H2O": "9.8",
      "mf": -2.81,
      "mu": 0.32,
      "CM_KIN": 3.12,
      "PhiF_H2O": 0.78,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.014",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "V6T",
      "MUTATION_PDB": "V6T",
      "SEC_STR": "Beta",
      "RSA": "1.4",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.39,
      "dln(kf)_H2O": -2.6,
      "ln(ku)_H2O": 0.67,
      "dln(ku)_H2O": 0.2,
      "dGKIN_H2O": "8.9",
      "mf": -3.22,
      "mu": 0.34,
      "CM_KIN": 2.51,
      "PhiF_H2O": 0.96,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.015",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "V6T",
      "MUTATION_PDB": "V6T",
      "SEC_STR": "Beta",
      "RSA": "1.4",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 4.39,
      "dln(kf)_H2O": -2.6,
      "ln(ku)_H2O": 0.67,
      "dln(ku)_H2O": 0.2,
      "dGKIN_H2O": "8.9",
      "mf": -3.22,
      "mu": 0.34,
      "CM_KIN": 2.51,
      "PhiF_H2O": 0.96,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
         "E3L"
      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.015",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "K7A",
      "MUTATION_PDB": "K7A",
      "SEC_STR": "Beta",
      "RSA": "36.6",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.27,
      "dln(kf)_H2O": -1.72,
      "ln(ku)_H2O": 0.67,
      "dln(ku)_H2O": 0.2,
      "dGKIN_H2O": "11",
      "mf": -2.59,
      "mu": 0.32,
      "CM_KIN": 3.78,
      "PhiF_H2O": 0.89,
      "BACKGROUND_MUT_UNIPROT": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.016",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1cspA00 (2.40.50.140)"
      ],
      "MUTATION_UNIPROT": "K7A",
      "MUTATION_PDB": "K7A",
      "SEC_STR": "Beta",
      "RSA": "36.6",
      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.27,
      "dln(kf)_H2O": -1.72,
      "ln(ku)_H2O": 0.67,
      "dln(ku)_H2O": 0.2,
      "dGKIN_H2O": "11",
      "mf": -2.59,
      "mu": 0.32,
      "CM_KIN": 3.78,
      "PhiF_H2O": 0.89,
      "BACKGROUND_MUT_UNIPROT": [
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      "BACKGROUND_MUT_PDB": [
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      ],
      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.016",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
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         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "N10A",
      "SEC_STR": "Beta",
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      "T": 15.0,
      "pH": 7.0,
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      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.017",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
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      "MUTATED_CHAIN": "A",
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      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.017",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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         "1cspA00 (2.40.50.140)"
      ],
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      "MUTATION_PDB": "E12A",
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      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.018",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "K13A",
      "SEC_STR": "Coil",
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      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.019",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
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         "1cspA00 (2.40.50.140)"
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      "SEC_STR": "Coil",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.019",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "F15A",
      "SEC_STR": "Beta",
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      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dln(ku)_H2O": 1.48,
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      "BACKGROUND_MUT_UNIPROT": [
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.020",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.020",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "F17A",
      "MUTATION_PDB": "F17A",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.021",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "F17A",
      "MUTATION_PDB": "F17A",
      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dln(ku)_H2O": 1.88,
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      "CM_KIN": 3.98,
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      "BACKGROUND_MUT_UNIPROT": [
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.021",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "I18V",
      "MUTATION_PDB": "I18V",
      "SEC_STR": "Beta",
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      "T": 15.0,
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      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
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      "BACKGROUND_MUT_UNIPROT": [
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.022",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "SEC_STR": "Beta",
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      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
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      "BACKGROUND_MUT_UNIPROT": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.022",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "E19A",
      "SEC_STR": "Beta",
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      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "dGKIN_H2O": "16",
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      "CM_KIN": 5.77,
      "PhiF_H2O": -0.5,
      "BACKGROUND_MUT_UNIPROT": [
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.023",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "UniProt": "P32081",
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      "PMID_KIN": "15147842",
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      "PMID_KIN": "15147842",
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      "UniProt": "P32081",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "UniProt": "P32081",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
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      "UniProt": "P32081",
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      "UniProt": "P32081",
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      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.027",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
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      "UniProt": "P32081",
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      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.028",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
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      "UniProt": "P32081",
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      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.029",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.029",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "F49A",
      "SEC_STR": "Beta",
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      "T": 15.0,
      "pH": 7.0,
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.030",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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         "1cspA00 (2.40.50.140)"
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.030",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "F49L",
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      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.031",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_PDB": "F49L",
      "SEC_STR": "Beta",
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      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.031",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "I51A",
      "MUTATION_PDB": "I51A",
      "SEC_STR": "Beta",
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      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "ln(ku)_H2O": 3.49,
      "dln(ku)_H2O": 3.02,
      "dGKIN_H2O": "7.3",
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      "CM_KIN": 2.79,
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.032",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "I51A",
      "MUTATION_PDB": "I51A",
      "SEC_STR": "Beta",
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      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
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      "MEASURE_KIN": "stopped-flow",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.032",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
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      "MUTATED_CHAIN": "A",
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      "MUTATION_PDB": "A60G",
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      "PhiF_H2O": 0.14,
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.033",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "BUFFER_NAME": "Sodium Cacodylate",
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      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.033",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
      "PDB_wild": "1csp",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "V63A",
      "MUTATION_PDB": "V63A",
      "SEC_STR": "Beta",
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      "T": 15.0,
      "pH": 7.0,
      "BUFFER_NAME": "Sodium Cacodylate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.25,
      "dln(kf)_H2O": -0.74,
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      "CM_KIN": 1.94,
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
      "REFERENCE_KIN": "The folding transition state of the cold shock protein is strongly polarized. J. Mol. Biol. 339, 555\u2013569. https://doi.org/10.1016/j.jmb.2004.04.034",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
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   {
      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
      "LENGTH": 67.0,
      "UniProt": "P32081",
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      "MUTATED_CHAIN": "A",
      "PFAM": [
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      "CATH": [
         "1cspA00 (2.40.50.140)"
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      "MUTATION_UNIPROT": "V63A",
      "MUTATION_PDB": "V63A",
      "SEC_STR": "Beta",
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      "BACKGROUND_MUT_PDB": [
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      "AUTHOR_KIN": "Garcia-Mira, M.M., Boehringer, D., Schmid, F.X.",
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      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 8.52,
      "ln(ku)_H2O": -6.44,
      "dGKIN_H2O": 34.5,
      "mf": -5.38,
      "mu": 3.63,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20340",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
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      "UniProt": "P31787",
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      "CATH": [
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      "MUTATION_UNIPROT": "WT",
      "MUTATION_PDB": "WT",
      "T": 5.0,
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      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 8.52,
      "ln(ku)_H2O": -6.44,
      "dGKIN_H2O": 34.5,
      "mf": -5.38,
      "mu": 3.63,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
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      "PMID_KIN": "15690348",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
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      "UniProt": "P31787",
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      "CATH": [
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      ],
      "MUTATION_UNIPROT": "F6A",
      "MUTATION_PDB": "F5A",
      "SEC_STR": "Helix",
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      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "PROTEIN": "yACBP",
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      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.88,
      "dln(kf)_H2O": -1.64,
      "ln(ku)_H2O": -2.26,
      "dln(ku)_H2O": 4.18,
      "dGKIN_H2O": 21.1,
      "ddGKIN_H2O": -13.4,
      "mf": -6.06,
      "mu": 2.89,
      "PhiF_H2O": 0.28,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20353",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y74A",
      "MUTATION_PDB": "Y73A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.12,
      "dln(kf)_H2O": -2.4,
      "ln(ku)_H2O": 0.13,
      "dln(ku)_H2O": 6.57,
      "dGKIN_H2O": 13.8,
      "ddGKIN_H2O": -20.7,
      "mf": -6.42,
      "mu": 2.39,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20354",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "Y74A",
      "MUTATION_PDB": "Y73A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 6.12,
      "dln(kf)_H2O": -2.4,
      "ln(ku)_H2O": 0.13,
      "dln(ku)_H2O": 6.57,
      "dGKIN_H2O": 13.8,
      "ddGKIN_H2O": -20.7,
      "mf": -6.42,
      "mu": 2.39,
      "PhiF_H2O": 0.27,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20354",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "I75A",
      "MUTATION_PDB": "I74A",
      "SEC_STR": "Helix",
      "RSA": "36.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.07,
      "dln(kf)_H2O": 0.55,
      "ln(ku)_H2O": -1.25,
      "dln(ku)_H2O": 5.19,
      "dGKIN_H2O": 23.8,
      "ddGKIN_H2O": -10.7,
      "mf": -6.2,
      "mu": 2.21,
      "PhiF_H2O": -0.12,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20355",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "I75A",
      "MUTATION_PDB": "I74A",
      "SEC_STR": "Helix",
      "RSA": "36.7",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 9.07,
      "dln(kf)_H2O": 0.55,
      "ln(ku)_H2O": -1.25,
      "dln(ku)_H2O": 5.19,
      "dGKIN_H2O": 23.8,
      "ddGKIN_H2O": -10.7,
      "mf": -6.2,
      "mu": 2.21,
      "PhiF_H2O": -0.12,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20355",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "V78A",
      "MUTATION_PDB": "V77A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.64,
      "dln(kf)_H2O": -0.88,
      "ln(ku)_H2O": -6.92,
      "dln(ku)_H2O": -0.48,
      "dGKIN_H2O": 33.6,
      "ddGKIN_H2O": -0.91,
      "mf": -5.69,
      "mu": 3.69,
      "PhiF_H2O": 2.24,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20356",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "V78A",
      "MUTATION_PDB": "V77A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 7.64,
      "dln(kf)_H2O": -0.88,
      "ln(ku)_H2O": -6.92,
      "dln(ku)_H2O": -0.48,
      "dGKIN_H2O": 33.6,
      "ddGKIN_H2O": -0.91,
      "mf": -5.69,
      "mu": 3.69,
      "PhiF_H2O": 2.24,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20356",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L81A",
      "MUTATION_PDB": "L80A",
      "SEC_STR": "Helix",
      "RSA": "4.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.61,
      "dln(kf)_H2O": -3.91,
      "ln(ku)_H2O": -5.09,
      "dln(ku)_H2O": 1.35,
      "dGKIN_H2O": 22.4,
      "ddGKIN_H2O": -12.1,
      "mf": -6.23,
      "mu": 3.84,
      "PhiF_H2O": 0.74,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20357",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "yACBP",
      "SOURCE": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker yeast)",
      "LENGTH": 79.0,
      "UniProt": "P31787",
      "PDB_wild": "1st7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00887"
      ],
      "CATH": [
         "1st7A00 (1.20.80.10)"
      ],
      "MUTATION_UNIPROT": "L81A",
      "MUTATION_PDB": "L80A",
      "SEC_STR": "Helix",
      "RSA": "4.3",
      "T": 5.0,
      "pH": 5.3,
      "BUFFER_NAME": "Na-acetate",
      "BUFFER_CONC": "0.02",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.61,
      "dln(kf)_H2O": -3.91,
      "ln(ku)_H2O": -5.09,
      "dln(ku)_H2O": 1.35,
      "dGKIN_H2O": 22.4,
      "ddGKIN_H2O": -12.1,
      "mf": -6.23,
      "mu": 3.84,
      "PhiF_H2O": 0.74,
      "AUTHOR_KIN": "Teilum, K., Thormann, T., Caterer, N.R., Poulsen, H.I., Jensen, P.H., Knudsen, J., Kragelund, B.B., Poulsen, F.M.",
      "REFERENCE_KIN": "Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles. Proteins 59, 80\u201390. https://doi.org/10.1002/prot.20357",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "15690348",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Cold shock-like protein",
      "SOURCE": "Thermotoga maritima",
      "LENGTH": 66.0,
      "UniProt": "O54310",
      "PDB_wild": "1g6p",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1g6pA00 (2.40.50.140)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Na cacodylate-HCI",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 6.34,
      "ln(ku)_H2O": -4.02,
      "dGKIN_H2O": 25.6,
      "AUTHOR_KIN": "Perl D, Welker C, Schindler T, Schr\u00f6der K, Marahiel MA, Jaenicke R, Schmid FX",
      "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9501917",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Cold shock-like protein",
      "SOURCE": "Thermotoga maritima",
      "LENGTH": 66.0,
      "UniProt": "O54310",
      "PDB_wild": "1g6p",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1g6pA00 (2.40.50.140)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Na cacodylate-HCI",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 6.34,
      "ln(ku)_H2O": -4.02,
      "dGKIN_H2O": 25.6,
      "AUTHOR_KIN": "Perl D, Welker C, Schindler T, Schr\u00f6der K, Marahiel MA, Jaenicke R, Schmid FX",
      "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9501917",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Cold shock protein CspA",
      "SOURCE": "Escherichia coli (strain K12)",
      "LENGTH": 69.0,
      "UniProt": "P0A9X9",
      "PDB_wild": "1mjc",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1mjcA00 (2.40.50.140)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "KPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.29,
      "ln(ku)_H2O": 1.44,
      "dGKIN_H2O": 9.54,
      "AUTHOR_KIN": "Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM",
      "REFERENCE_KIN": "Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7(2):470-9",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9521124",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Cold shock protein CspA",
      "SOURCE": "Escherichia coli (strain K12)",
      "LENGTH": 69.0,
      "UniProt": "P0A9X9",
      "PDB_wild": "1mjc",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00313"
      ],
      "CATH": [
         "1mjcA00 (2.40.50.140)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "KPi",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.29,
      "ln(ku)_H2O": 1.44,
      "dGKIN_H2O": 9.54,
      "AUTHOR_KIN": "Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM",
      "REFERENCE_KIN": "Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7(2):470-9",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9521124",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Phosphocarrier protein HPr",
      "SOURCE": "Escherichia coli (strain K12)",
      "LENGTH": 85.0,
      "UniProt": "P0AA04",
      "PDB_wild": "1opd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00381"
      ],
      "CATH": [
         "1opdA00 (3.30.1340.10)"
      ],
      "MUTATION_PDB": "WT",
      "T": 20.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdnHCl",
      "ln(kf)_H2O": 2.7,
      "ln(ku)_H2O": -6.17,
      "dGKIN_H2O": 21.61,
      "AUTHOR_KIN": "Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM",
      "REFERENCE_KIN": "Slow cooperative folding of a small globular protein HPr. Biochemistry. 37(2):622-37",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9425085",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Phosphocarrier protein HPr",
      "SOURCE": "Escherichia coli (strain K12)",
      "LENGTH": 85.0,
      "UniProt": "P0AA04",
      "PDB_wild": "1opd",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00381"
      ],
      "CATH": [
         "1opdA00 (3.30.1340.10)"
      ],
      "MUTATION_PDB": "WT",
      "T": 20.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdnHCl",
      "ln(kf)_H2O": 2.7,
      "ln(ku)_H2O": -6.17,
      "dGKIN_H2O": 21.61,
      "AUTHOR_KIN": "Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM",
      "REFERENCE_KIN": "Slow cooperative folding of a small globular protein HPr. Biochemistry. 37(2):622-37",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9425085",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "TRF1 Myb domain (Telomeric repeat-binding factor 1)",
      "SOURCE": "Homo sapiens",
      "LENGTH": 53.0,
      "UniProt": "P54274",
      "PDB_wild": "1ba5",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00249"
      ],
      "CATH": [
         "1ba5A00 (1.10.10.60)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.91,
      "ln(ku)_H2O": 1.16,
      "dGKIN_H2O": 11.8,
      "mf": -3.6,
      "mu": 0.38,
      "beta-T": 0.9,
      "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR",
      "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "14595026",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "TRF1 Myb domain (Telomeric repeat-binding factor 1)",
      "SOURCE": "Homo sapiens",
      "LENGTH": 53.0,
      "UniProt": "P54274",
      "PDB_wild": "1ba5",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00249"
      ],
      "CATH": [
         "1ba5A00 (1.10.10.60)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 5.91,
      "ln(ku)_H2O": 1.16,
      "dGKIN_H2O": 11.8,
      "mf": -3.6,
      "mu": 0.38,
      "beta-T": 0.9,
      "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR",
      "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "14595026",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "RAP1 Myb domain (Telomeric repeat-binding factor 2-interacting protein 1)",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "Q9NYB0",
      "PDB_wild": "1fex",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF08914"
      ],
      "CATH": [
         "1fexA00 (1.10.10.60)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.73,
      "ln(ku)_H2O": 2.89,
      "dGKIN_H2O": 13.05,
      "mf": -2.85,
      "mu": 0.63,
      "beta-T": 0.82,
      "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR",
      "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "14595026",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "RAP1 Myb domain (Telomeric repeat-binding factor 2-interacting protein 1)",
      "SOURCE": "Homo sapiens",
      "LENGTH": 59.0,
      "UniProt": "Q9NYB0",
      "PDB_wild": "1fex",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF08914"
      ],
      "CATH": [
         "1fexA00 (1.10.10.60)"
      ],
      "MUTATION_PDB": "WT",
      "T": 25.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.73,
      "ln(ku)_H2O": 2.89,
      "dGKIN_H2O": 13.05,
      "mf": -2.85,
      "mu": 0.63,
      "beta-T": 0.82,
      "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR",
      "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "14595026",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "c-Myb-transforming protein (Transcriptional activator Myb)",
      "SOURCE": "Mus musculus",
      "LENGTH": 53.0,
      "UniProt": "P06876",
      "PDB_wild": "1idy",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00249"
      ],
      "CATH": [
         "1idyA00 (1.10.10.60)"
      ],
      "MUTATION_PDB": "WT(I155L)",
      "T": 25.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.19,
      "ln(ku)_H2O": 1.67,
      "dGKIN_H2O": 17.45,
      "mf": -2.72,
      "mu": 0.71,
      "beta-T": 0.79,
      "BACKGROUND_MUT_PDB": [
         "I155L"
      ],
      "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR",
      "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "14595026",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "c-Myb-transforming protein (Transcriptional activator Myb)",
      "SOURCE": "Mus musculus",
      "LENGTH": 53.0,
      "UniProt": "P06876",
      "PDB_wild": "1idy",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00249"
      ],
      "CATH": [
         "1idyA00 (1.10.10.60)"
      ],
      "MUTATION_PDB": "WT(I155L)",
      "T": 25.0,
      "pH": 5.7,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 8.19,
      "ln(ku)_H2O": 1.67,
      "dGKIN_H2O": 17.45,
      "mf": -2.72,
      "mu": 0.71,
      "beta-T": 0.79,
      "BACKGROUND_MUT_PDB": [
         "I155L"
      ],
      "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR",
      "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100",
      "YEAR_KIN": 2003.0,
      "PMID_KIN": "14595026",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "18th module of muscle protein twitchin",
      "SOURCE": "Caenorhabditis elegans",
      "LENGTH": 93.0,
      "UniProt": "Q23551",
      "PDB_wild": "1wit",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF07679"
      ],
      "CATH": [
         "1witA00 (2.60.40.10)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_PDB": "WT",
      "T": 20.0,
      "pH": 5.0,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 0.41,
      "ln(ku)_H2O": -8.18,
      "dGKIN_H2O": 20.93,
      "beta-T": 0.7,
      "AUTHOR_KIN": "Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J   Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39",
      "REFERENCE_KIN": "Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39. https://doi.org/10.1006/jmbi.1996.0665",
      "YEAR_KIN": 1996.0,
      "PMID_KIN": "8969309",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "18th module of muscle protein twitchin",
      "SOURCE": "Caenorhabditis elegans",
      "LENGTH": 93.0,
      "UniProt": "Q23551",
      "PDB_wild": "1wit",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF07679"
      ],
      "CATH": [
         "1witA00 (2.60.40.10)"
      ],
      "EC_NUMBER": "2.7.11.1",
      "MUTATION_PDB": "WT",
      "T": 20.0,
      "pH": 5.0,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 0.41,
      "ln(ku)_H2O": -8.18,
      "dGKIN_H2O": 20.93,
      "beta-T": 0.7,
      "AUTHOR_KIN": "Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J   Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39",
      "REFERENCE_KIN": "Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39. https://doi.org/10.1006/jmbi.1996.0665",
      "YEAR_KIN": 1996.0,
      "PMID_KIN": "8969309",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Acylphosphatase-1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 99.0,
      "UniProt": "P07311",
      "PDB_wild": "2vh7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "CATH": [
         "2vh7A00 (3.30.70.100)"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_PDB": "WT",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.84,
      "ln(ku)_H2O": -6.5,
      "dGKIN_H2O": 18.37,
      "mf": -5.1,
      "mu": 2.0,
      "CM_KIN": 2.6,
      "AUTHOR_KIN": "Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G",
      "REFERENCE_KIN": "Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38(7):2135-42. https://doi.org/10.1021/bi9822630",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10026297",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Acylphosphatase-1",
      "SOURCE": "Homo sapiens",
      "LENGTH": 99.0,
      "UniProt": "P07311",
      "PDB_wild": "2vh7",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00708"
      ],
      "CATH": [
         "2vh7A00 (3.30.70.100)"
      ],
      "EC_NUMBER": "3.6.1.7",
      "MUTATION_PDB": "WT",
      "T": 28.0,
      "pH": 5.5,
      "BUFFER_NAME": "Na Acetate",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 0.84,
      "ln(ku)_H2O": -6.5,
      "dGKIN_H2O": 18.37,
      "mf": -5.1,
      "mu": 2.0,
      "CM_KIN": 2.6,
      "AUTHOR_KIN": "Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G",
      "REFERENCE_KIN": "Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38(7):2135-42. https://doi.org/10.1021/bi9822630",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10026297",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "apocytochrome b5",
      "SOURCE": "Bos taurus",
      "LENGTH": 93.0,
      "UniProt": "P00171",
      "PDB_wild": "1cyo",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00173"
      ],
      "CATH": [
         "1cyoA00 (3.10.120.10)"
      ],
      "MUTATION_PDB": "WT",
      "T": 10.0,
      "pH": 7.0,
      "BUFFER_NAME": "MOPS",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 2.97,
      "ln(ku)_H2O": -1.43,
      "dGKIN_H2O": 10.35,
      "mf": -5.59,
      "mu": 2.4,
      "CM_KIN": 1.58,
      "AUTHOR_KIN": "Manyusa S, Whitford D",
      "REFERENCE_KIN": "Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements. Biochemistry 38(29):9533-40. https://doi.org/10.1021/bi990550d",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10413531",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "apocytochrome b5",
      "SOURCE": "Bos taurus",
      "LENGTH": 93.0,
      "UniProt": "P00171",
      "PDB_wild": "1cyo",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00173"
      ],
      "CATH": [
         "1cyoA00 (3.10.120.10)"
      ],
      "MUTATION_PDB": "WT",
      "T": 10.0,
      "pH": 7.0,
      "BUFFER_NAME": "MOPS",
      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GdmCl",
      "ln(kf)_H2O": 2.97,
      "ln(ku)_H2O": -1.43,
      "dGKIN_H2O": 10.35,
      "mf": -5.59,
      "mu": 2.4,
      "CM_KIN": 1.58,
      "AUTHOR_KIN": "Manyusa S, Whitford D",
      "REFERENCE_KIN": "Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements. Biochemistry 38(29):9533-40. https://doi.org/10.1021/bi990550d",
      "YEAR_KIN": 1999.0,
      "PMID_KIN": "10413531",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Villin-1",
      "SOURCE": "Gallus gallus",
      "LENGTH": 126.0,
      "UniProt": "P02640",
      "PDB_wild": "2vik",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00626"
      ],
      "CATH": [
         "2vikA00 (3.40.20.10)"
      ],
      "MUTATION_PDB": "WT",
      "T": 37.0,
      "pH": 4.1,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM beta-ME",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.8,
      "ln(ku)_H2O": -2.8,
      "dGKIN_H2O": 24.74,
      "mf": -4.64,
      "mu": 1.72,
      "AUTHOR_KIN": "Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI",
      "REFERENCE_KIN": "Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry. 37(41):14508-18. https://doi.org/10.1021/bi980889k",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9772179",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Villin-1",
      "SOURCE": "Gallus gallus",
      "LENGTH": 126.0,
      "UniProt": "P02640",
      "PDB_wild": "2vik",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00626"
      ],
      "CATH": [
         "2vikA00 (3.40.20.10)"
      ],
      "MUTATION_PDB": "WT",
      "T": 37.0,
      "pH": 4.1,
      "BUFFER_NAME": "Acetate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "1 mM beta-ME",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
      "ln(kf)_H2O": 6.8,
      "ln(ku)_H2O": -2.8,
      "dGKIN_H2O": 24.74,
      "mf": -4.64,
      "mu": 1.72,
      "AUTHOR_KIN": "Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI",
      "REFERENCE_KIN": "Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry. 37(41):14508-18. https://doi.org/10.1021/bi980889k",
      "YEAR_KIN": 1998.0,
      "PMID_KIN": "9772179",
      "STATE": "Yes",
      "REVIEW_DATE": "2023-06-09T01:00:00"
   },
   {
      "PROTEIN": "Azurin",
      "SOURCE": "Pseudomonas aeruginosa",
      "LENGTH": 128.0,
      "UniProt": "P00282",
      "PDB_wild": "1azu",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00127"
      ],
      "CATH": [
         "1azuA00 (2.60.40.420)"
      ],
      "MUTATION_UNIPROT": "L145A",
      "MUTATION_PDB": "L125A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "TRIS",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.78,
      "dln(kf)_H2O": -1.06,
      "ln(ku)_H2O": -15.19,
      "dln(ku)_H2O": 1.77,
      "PhiF_H2O": 0.36,
      "AUTHOR_KIN": "Wilson, C.J., Wittung-Stafshede, P.",
      "REFERENCE_KIN": "Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054\u201310062. https://doi.org/10.1021/bi050342n",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "16042382",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Azurin",
      "SOURCE": "Pseudomonas aeruginosa",
      "LENGTH": 128.0,
      "UniProt": "P00282",
      "PDB_wild": "1azu",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00127"
      ],
      "CATH": [
         "1azuA00 (2.60.40.420)"
      ],
      "MUTATION_UNIPROT": "L145A",
      "MUTATION_PDB": "L125A",
      "SEC_STR": "Beta",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "TRIS",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 3.78,
      "dln(kf)_H2O": -1.06,
      "ln(ku)_H2O": -15.19,
      "dln(ku)_H2O": 1.77,
      "PhiF_H2O": 0.36,
      "AUTHOR_KIN": "Wilson, C.J., Wittung-Stafshede, P.",
      "REFERENCE_KIN": "Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054\u201310062. https://doi.org/10.1021/bi050342n",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "16042382",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
   {
      "PROTEIN": "Azurin",
      "SOURCE": "Pseudomonas aeruginosa",
      "LENGTH": 128.0,
      "UniProt": "P00282",
      "PDB_wild": "1azu",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00127"
      ],
      "CATH": [
         "1azuA00 (2.60.40.420)"
      ],
      "MUTATION_UNIPROT": "I27A",
      "MUTATION_PDB": "I7A",
      "SEC_STR": "Beta",
      "RSA": "1.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "TRIS",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.39,
      "dln(kf)_H2O": -0.45,
      "ln(ku)_H2O": -11.75,
      "dln(ku)_H2O": 5.21,
      "PhiF_H2O": 0.08,
      "AUTHOR_KIN": "Wilson, C.J., Wittung-Stafshede, P.",
      "REFERENCE_KIN": "Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054\u201310062. https://doi.org/10.1021/bi050342n",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "pH": 7.0,
      "BUFFER_NAME": "TRIS",
      "BUFFER_CONC": "0.1",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "GuHCl",
      "ln(kf)_H2O": 4.6,
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      "ln(ku)_H2O": -15.59,
      "dln(ku)_H2O": 1.37,
      "PhiF_H2O": 0.15,
      "AUTHOR_KIN": "Wilson, C.J., Wittung-Stafshede, P.",
      "REFERENCE_KIN": "Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054\u201310062. https://doi.org/10.1021/bi050342n",
      "YEAR_KIN": 2005.0,
      "PMID_KIN": "16042382",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
   },
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      "SOURCE": "Mus musculus",
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      "UniProt": "P45481",
      "PDB_wild": "1sb0",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF02172"
      ],
      "CATH": [
         "1sb0A00 (1.10.246.20)"
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      "EC_NUMBER": "2.3.1.48",
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      "MUTATION_PDB": "WT",
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      "BUFFER_CONC": "0.05",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "urea",
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      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
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         "1sb0A00 (1.10.246.20)"
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      "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289",
      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
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         "1sb0A00 (1.10.246.20)"
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      "YEAR_KIN": 2017.0,
      "PMID_KIN": "28459531",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
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      "PDB_wild": "1sb0",
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         "1sb0A00 (1.10.246.20)"
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      "EC_NUMBER": "2.3.1.48",
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      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
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      "PMID_KIN": "28459531",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
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         "1sb0A00 (1.10.246.20)"
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      "EC_NUMBER": "2.3.1.48",
      "MUTATION_UNIPROT": "L599A",
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      "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S",
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      "PMID_KIN": "28459531",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
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         "1sb0A00 (1.10.246.20)"
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      "EC_NUMBER": "2.3.1.48",
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      "PMID_KIN": "28459531",
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      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
      "LENGTH": 86.0,
      "UniProt": "P45481",
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         "1sb0A00 (1.10.246.20)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Mus musculus",
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         "1sb0A00 (1.10.246.20)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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   {
      "PROTEIN": "CBP, KIX domain",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
      "SOURCE": "Mus musculus",
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         "1sb0A00 (1.10.246.20)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "CBP, KIX domain",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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         "1sb0A00 (1.10.246.20)"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
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         "1sb0A00 (1.10.246.20)"
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]