[ { "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": "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": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.09, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 27.1, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.09, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 27.1, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L3A", "MUTATION_PDB": "L3A", "SEC_STR": "Coil", "RSA": "61.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.75, "dln(kf)_H2O": -0.34, "ln(ku)_H2O": -4.02, "dln(ku)_H2O": 0.4, "dGKIN_H2O": 25.0, "ddGKIN_H2O": -2.1, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L3A", "MUTATION_PDB": "L3A", "SEC_STR": "Coil", "RSA": "61.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.75, "dln(kf)_H2O": -0.34, "ln(ku)_H2O": -4.02, "dln(ku)_H2O": 0.4, "dGKIN_H2O": 25.0, "ddGKIN_H2O": -2.1, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I7V", "MUTATION_PDB": "I7V", "SEC_STR": "Coil", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -1.9, "dln(ku)_H2O": 2.52, "dGKIN_H2O": 20.0, "ddGKIN_H2O": -7.1, "PhiF_H2O": 0.15, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I7V", "MUTATION_PDB": "I7V", "SEC_STR": "Coil", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -1.9, "dln(ku)_H2O": 2.52, "dGKIN_H2O": 20.0, "ddGKIN_H2O": -7.1, "PhiF_H2O": 0.15, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A13G", "MUTATION_PDB": "A13G", "SEC_STR": "Helix", "RSA": "50.9", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.7, "dln(kf)_H2O": -1.39, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 23.8, "ddGKIN_H2O": -3.3, "PhiF_H2O": 0.98, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A13G", "MUTATION_PDB": "A13G", "SEC_STR": "Helix", "RSA": "50.9", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.7, "dln(kf)_H2O": -1.39, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 23.8, "ddGKIN_H2O": -3.3, "PhiF_H2O": 0.98, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "F15A", "MUTATION_PDB": "F15A", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 1.86, "dln(kf)_H2O": -5.23, "ln(ku)_H2O": -0.82, "dln(ku)_H2O": 3.6, "dGKIN_H2O": 6.3, "ddGKIN_H2O": -20.8, "PhiF_H2O": 0.57, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "F15A", "MUTATION_PDB": "F15A", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 1.86, "dln(kf)_H2O": -5.23, "ln(ku)_H2O": -0.82, "dln(ku)_H2O": 3.6, "dGKIN_H2O": 6.3, "ddGKIN_H2O": -20.8, "PhiF_H2O": 0.57, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L16A", "MUTATION_PDB": "L16A", "SEC_STR": "Helix", "RSA": "23.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.35, "dln(kf)_H2O": -1.74, "ln(ku)_H2O": -3.08, "dln(ku)_H2O": 1.34, "dGKIN_H2O": 19.8, "ddGKIN_H2O": -7.3, "PhiF_H2O": 0.52, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L16A", "MUTATION_PDB": "L16A", "SEC_STR": "Helix", "RSA": "23.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.35, "dln(kf)_H2O": -1.74, "ln(ku)_H2O": -3.08, "dln(ku)_H2O": 1.34, "dGKIN_H2O": 19.8, "ddGKIN_H2O": -7.3, "PhiF_H2O": 0.52, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L18A", "MUTATION_PDB": "L18A", "SEC_STR": "Helix", "RSA": "11.6", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 4.44, "dln(kf)_H2O": -2.65, "ln(ku)_H2O": -0.87, "dln(ku)_H2O": 3.55, "dGKIN_H2O": 12.7, "ddGKIN_H2O": -14.4, "PhiF_H2O": 0.4, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L18A", "MUTATION_PDB": "L18A", "SEC_STR": "Helix", "RSA": "11.6", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 4.44, "dln(kf)_H2O": -2.65, "ln(ku)_H2O": -0.87, "dln(ku)_H2O": 3.55, "dGKIN_H2O": 12.7, "ddGKIN_H2O": -14.4, "PhiF_H2O": 0.4, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V19A", "MUTATION_PDB": "V19A", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.08, "dln(kf)_H2O": -2.01, "ln(ku)_H2O": -0.69, "dln(ku)_H2O": 3.73, "dGKIN_H2O": 13.6, "ddGKIN_H2O": -13.5, "PhiF_H2O": 0.32, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V19A", "MUTATION_PDB": "V19A", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.08, "dln(kf)_H2O": -2.01, "ln(ku)_H2O": -0.69, "dln(ku)_H2O": 3.73, "dGKIN_H2O": 13.6, "ddGKIN_H2O": -13.5, "PhiF_H2O": 0.32, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T21A", "MUTATION_PDB": "T21A", "SEC_STR": "Helix", "RSA": "33.1", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.65, "dln(kf)_H2O": 0.56, "ln(ku)_H2O": -3.73, "dln(ku)_H2O": 0.69, "dGKIN_H2O": 26.78, "ddGKIN_H2O": -0.32, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T21A", "MUTATION_PDB": "T21A", "SEC_STR": "Helix", "RSA": "33.1", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.65, "dln(kf)_H2O": 0.56, "ln(ku)_H2O": -3.73, "dln(ku)_H2O": 0.69, "dGKIN_H2O": 26.78, "ddGKIN_H2O": -0.32, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T21G", "MUTATION_PDB": "T21G", "SEC_STR": "Helix", "RSA": "33.1", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.17, "dln(kf)_H2O": -0.92, "ln(ku)_H2O": -2.32, "dln(ku)_H2O": 2.1, "dGKIN_H2O": 19.99, "ddGKIN_H2O": -7.11, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T21G", "MUTATION_PDB": "T21G", "SEC_STR": "Helix", "RSA": "33.1", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.17, "dln(kf)_H2O": -0.92, "ln(ku)_H2O": -2.32, "dln(ku)_H2O": 2.1, "dGKIN_H2O": 19.99, "ddGKIN_H2O": -7.11, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T21S", "MUTATION_PDB": "T21S", "SEC_STR": "Helix", "RSA": "33.1", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.17, "dln(kf)_H2O": 0.08, "ln(ku)_H2O": -3.17, "dln(ku)_H2O": 1.25, "dGKIN_H2O": 24.3, "ddGKIN_H2O": -2.8, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T21S", "MUTATION_PDB": "T21S", "SEC_STR": "Helix", "RSA": "33.1", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.17, "dln(kf)_H2O": 0.08, "ln(ku)_H2O": -3.17, "dln(ku)_H2O": 1.25, "dGKIN_H2O": 24.3, "ddGKIN_H2O": -2.8, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I22V", "MUTATION_PDB": "I22V", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.89, "dln(kf)_H2O": -1.2, "ln(ku)_H2O": -1.83, "dln(ku)_H2O": 2.59, "dGKIN_H2O": 18.2, "ddGKIN_H2O": -8.9, "PhiF_H2O": 0.31, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I22V", "MUTATION_PDB": "I22V", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.89, "dln(kf)_H2O": -1.2, "ln(ku)_H2O": -1.83, "dln(ku)_H2O": 2.59, "dGKIN_H2O": 18.2, "ddGKIN_H2O": -8.9, "PhiF_H2O": 0.31, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A25G", "MUTATION_PDB": "A25G", "SEC_STR": "Coil", "RSA": "67.9", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.38, "dln(kf)_H2O": 0.29, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 27.8, "ddGKIN_H2O": 0.7, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A25G", "MUTATION_PDB": "A25G", "SEC_STR": "Coil", "RSA": "67.9", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.38, "dln(kf)_H2O": 0.29, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 27.8, "ddGKIN_H2O": 0.7, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T27S", "MUTATION_PDB": "T27S", "SEC_STR": "Coil", "RSA": "18.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.18, "ln(ku)_H2O": -3.1, "dln(ku)_H2O": 1.32, "dGKIN_H2O": 23.6, "ddGKIN_H2O": -3.5, "PhiF_H2O": 0.12, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T27S", "MUTATION_PDB": "T27S", "SEC_STR": "Coil", "RSA": "18.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.18, "ln(ku)_H2O": -3.1, "dln(ku)_H2O": 1.32, "dGKIN_H2O": 23.6, "ddGKIN_H2O": -3.5, "PhiF_H2O": 0.12, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L33A", "MUTATION_PDB": "L33A", "SEC_STR": "Helix", "RSA": "9.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.89, "dln(kf)_H2O": -1.2, "ln(ku)_H2O": -1.35, "dln(ku)_H2O": 3.07, "dGKIN_H2O": 17.0, "ddGKIN_H2O": -10.1, "PhiF_H2O": 0.27, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L33A", "MUTATION_PDB": "L33A", "SEC_STR": "Helix", "RSA": "9.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.89, "dln(kf)_H2O": -1.2, "ln(ku)_H2O": -1.35, "dln(ku)_H2O": 3.07, "dGKIN_H2O": 17.0, "ddGKIN_H2O": -10.1, "PhiF_H2O": 0.27, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V34A", "MUTATION_PDB": "V34A", "SEC_STR": "Helix", "RSA": "49.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.55, "dln(kf)_H2O": 0.46, "ln(ku)_H2O": -4.89, "dln(ku)_H2O": -0.47, "dGKIN_H2O": 29.2, "ddGKIN_H2O": 2.1, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V34A", "MUTATION_PDB": "V34A", "SEC_STR": "Helix", "RSA": "49.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.55, "dln(kf)_H2O": 0.46, "ln(ku)_H2O": -4.89, "dln(ku)_H2O": -0.47, "dGKIN_H2O": 29.2, "ddGKIN_H2O": 2.1, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V34G", "MUTATION_PDB": "V34G", "SEC_STR": "Helix", "RSA": "49.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -4.51, "dln(ku)_H2O": -0.09, "dGKIN_H2O": 26.19, "ddGKIN_H2O": -0.91, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V34G", "MUTATION_PDB": "V34G", "SEC_STR": "Helix", "RSA": "49.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -4.51, "dln(ku)_H2O": -0.09, "dGKIN_H2O": 26.19, "ddGKIN_H2O": -0.91, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L36A", "MUTATION_PDB": "L36A", "SEC_STR": "Helix", "RSA": "21.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.99, "dln(kf)_H2O": -1.1, "ln(ku)_H2O": -1.31, "dln(ku)_H2O": 3.11, "dGKIN_H2O": 17.2, "ddGKIN_H2O": -9.9, "PhiF_H2O": 0.25, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L36A", "MUTATION_PDB": "L36A", "SEC_STR": "Helix", "RSA": "21.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.99, "dln(kf)_H2O": -1.1, "ln(ku)_H2O": -1.31, "dln(ku)_H2O": 3.11, "dGKIN_H2O": 17.2, "ddGKIN_H2O": -9.9, "PhiF_H2O": 0.25, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V37A", "MUTATION_PDB": "V37A", "SEC_STR": "Helix", "RSA": "1.4", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -1.97, "dln(ku)_H2O": 2.45, "dGKIN_H2O": 20.2, "ddGKIN_H2O": -6.9, "PhiF_H2O": 0.15, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V37A", "MUTATION_PDB": "V37A", "SEC_STR": "Helix", "RSA": "1.4", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -1.97, "dln(ku)_H2O": 2.45, "dGKIN_H2O": 20.2, "ddGKIN_H2O": -6.9, "PhiF_H2O": 0.15, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T38A", "MUTATION_PDB": "T38A", "SEC_STR": "Helix", "RSA": "52.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.82, "dln(kf)_H2O": 0.73, "ln(ku)_H2O": -3.77, "dln(ku)_H2O": 0.65, "dGKIN_H2O": 27.29, "ddGKIN_H2O": 0.19, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T38A", "MUTATION_PDB": "T38A", "SEC_STR": "Helix", "RSA": "52.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.82, "dln(kf)_H2O": 0.73, "ln(ku)_H2O": -3.77, "dln(ku)_H2O": 0.65, "dGKIN_H2O": 27.29, "ddGKIN_H2O": 0.19, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T38G", "MUTATION_PDB": "T38G", "SEC_STR": "Helix", "RSA": "52.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.8, "dln(kf)_H2O": -0.29, "ln(ku)_H2O": -4.14, "dln(ku)_H2O": 0.28, "dGKIN_H2O": 25.74, "ddGKIN_H2O": -1.36, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T38G", "MUTATION_PDB": "T38G", "SEC_STR": "Helix", "RSA": "52.8", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.8, "dln(kf)_H2O": -0.29, "ln(ku)_H2O": -4.14, "dln(ku)_H2O": 0.28, "dGKIN_H2O": 25.74, "ddGKIN_H2O": -1.36, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "F40L", "MUTATION_PDB": "F40L", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.0, "dln(kf)_H2O": -0.09, "ln(ku)_H2O": 1.95, "dln(ku)_H2O": 6.37, "dGKIN_H2O": 11.9, "ddGKIN_H2O": -15.2, "PhiF_H2O": 0.01, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "F40L", "MUTATION_PDB": "F40L", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.0, "dln(kf)_H2O": -0.09, "ln(ku)_H2O": 1.95, "dln(ku)_H2O": 6.37, "dGKIN_H2O": 11.9, "ddGKIN_H2O": -15.2, "PhiF_H2O": 0.01, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T44S", "MUTATION_PDB": "T44S", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -5.65, "dln(ku)_H2O": -1.23, "dGKIN_H2O": 28.8, "ddGKIN_H2O": 1.7, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "T44S", "MUTATION_PDB": "T44S", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.62, "dln(kf)_H2O": -0.47, "ln(ku)_H2O": -5.65, "dln(ku)_H2O": -1.23, "dGKIN_H2O": 28.8, "ddGKIN_H2O": 1.7, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L52A", "MUTATION_PDB": "L52A", "SEC_STR": "Helix", "RSA": "12.2", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.18, "ln(ku)_H2O": 1.9, "dln(ku)_H2O": 6.32, "dGKIN_H2O": 11.8, "ddGKIN_H2O": -15.3, "PhiF_H2O": 0.03, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "L52A", "MUTATION_PDB": "L52A", "SEC_STR": "Helix", "RSA": "12.2", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.18, "ln(ku)_H2O": 1.9, "dln(ku)_H2O": 6.32, "dGKIN_H2O": 11.8, "ddGKIN_H2O": -15.3, "PhiF_H2O": 0.03, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I53V", "MUTATION_PDB": "I53V", "SEC_STR": "Helix", "RSA": "8.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.18, "ln(ku)_H2O": -1.97, "dln(ku)_H2O": 2.45, "dGKIN_H2O": 20.9, "ddGKIN_H2O": -6.2, "PhiF_H2O": 0.07, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I53V", "MUTATION_PDB": "I53V", "SEC_STR": "Helix", "RSA": "8.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.18, "ln(ku)_H2O": -1.97, "dln(ku)_H2O": 2.45, "dGKIN_H2O": 20.9, "ddGKIN_H2O": -6.2, "PhiF_H2O": 0.07, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I67V", "MUTATION_PDB": "I67V", "SEC_STR": "Helix", "RSA": "2.4", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.11, "dln(kf)_H2O": -0.98, "ln(ku)_H2O": -3.22, "dln(ku)_H2O": 1.2, "dGKIN_H2O": 21.9, "ddGKIN_H2O": -5.2, "PhiF_H2O": 0.41, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "I67V", "MUTATION_PDB": "I67V", "SEC_STR": "Helix", "RSA": "2.4", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.11, "dln(kf)_H2O": -0.98, "ln(ku)_H2O": -3.22, "dln(ku)_H2O": 1.2, "dGKIN_H2O": 21.9, "ddGKIN_H2O": -5.2, "PhiF_H2O": 0.41, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V68A", "MUTATION_PDB": "V68A", "SEC_STR": "Helix", "RSA": "1.4", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.02, "dln(kf)_H2O": -1.07, "ln(ku)_H2O": -1.31, "dln(ku)_H2O": 3.11, "dGKIN_H2O": 17.2, "ddGKIN_H2O": -9.9, "PhiF_H2O": 0.23, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V68A", "MUTATION_PDB": "V68A", "SEC_STR": "Helix", "RSA": "1.4", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.02, "dln(kf)_H2O": -1.07, "ln(ku)_H2O": -1.31, "dln(ku)_H2O": 3.11, "dGKIN_H2O": 17.2, "ddGKIN_H2O": -9.9, "PhiF_H2O": 0.23, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "N69A", "MUTATION_PDB": "N69A", "SEC_STR": "Helix", "RSA": "50.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.31, "dln(kf)_H2O": 0.22, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 27.62, "ddGKIN_H2O": 0.52, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "N69A", "MUTATION_PDB": "N69A", "SEC_STR": "Helix", "RSA": "50.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.31, "dln(kf)_H2O": 0.22, "ln(ku)_H2O": -4.42, "dGKIN_H2O": 27.62, "ddGKIN_H2O": 0.52, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "N69G", "MUTATION_PDB": "N69G", "SEC_STR": "Helix", "RSA": "50.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.06, "dln(kf)_H2O": -1.03, "ln(ku)_H2O": -4.07, "dln(ku)_H2O": 0.35, "dGKIN_H2O": 23.86, "ddGKIN_H2O": -3.24, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "N69G", "MUTATION_PDB": "N69G", "SEC_STR": "Helix", "RSA": "50.3", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.06, "dln(kf)_H2O": -1.03, "ln(ku)_H2O": -4.07, "dln(ku)_H2O": 0.35, "dGKIN_H2O": 23.86, "ddGKIN_H2O": -3.24, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V71A", "MUTATION_PDB": "V71A", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.14, "dln(kf)_H2O": -1.95, "ln(ku)_H2O": -1.31, "dln(ku)_H2O": 3.11, "dGKIN_H2O": 15.2, "ddGKIN_H2O": -11.9, "PhiF_H2O": 0.36, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "V71A", "MUTATION_PDB": "V71A", "SEC_STR": "Helix", "RSA": "0.0", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.14, "dln(kf)_H2O": -1.95, "ln(ku)_H2O": -1.31, "dln(ku)_H2O": 3.11, "dGKIN_H2O": 15.2, "ddGKIN_H2O": -11.9, "PhiF_H2O": 0.36, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A76G", "MUTATION_PDB": "A76G", "SEC_STR": "Helix", "RSA": "80.2", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.21, "dln(kf)_H2O": -0.88, "ln(ku)_H2O": -3.08, "dln(ku)_H2O": 1.34, "dGKIN_H2O": 21.9, "ddGKIN_H2O": -5.2, "PhiF_H2O": 0.37, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A76G", "MUTATION_PDB": "A76G", "SEC_STR": "Helix", "RSA": "80.2", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.21, "dln(kf)_H2O": -0.88, "ln(ku)_H2O": -3.08, "dln(ku)_H2O": 1.34, "dGKIN_H2O": 21.9, "ddGKIN_H2O": -5.2, "PhiF_H2O": 0.37, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A77G", "MUTATION_PDB": "A77G", "SEC_STR": "Helix", "RSA": "74.5", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.21, "dln(kf)_H2O": -0.88, "ln(ku)_H2O": -3.32, "dln(ku)_H2O": 1.1, "dGKIN_H2O": 22.4, "ddGKIN_H2O": -4.7, "PhiF_H2O": 0.37, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "A77G", "MUTATION_PDB": "A77G", "SEC_STR": "Helix", "RSA": "74.5", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.21, "dln(kf)_H2O": -0.88, "ln(ku)_H2O": -3.32, "dln(ku)_H2O": 1.1, "dGKIN_H2O": 22.4, "ddGKIN_H2O": -4.7, "PhiF_H2O": 0.37, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "F83A", "MUTATION_PDB": "F83A", "SEC_STR": "Coil", "RSA": "12.2", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 4.25, "dln(kf)_H2O": -2.84, "ln(ku)_H2O": 1.65, "dln(ku)_H2O": 6.07, "dGKIN_H2O": 6.1, "ddGKIN_H2O": -21.0, "PhiF_H2O": 0.31, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "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": "F83A", "MUTATION_PDB": "F83A", "SEC_STR": "Coil", "RSA": "12.2", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "2 mM DTT, 1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 4.25, "dln(kf)_H2O": -2.84, "ln(ku)_H2O": 1.65, "dln(ku)_H2O": 6.07, "dGKIN_H2O": 6.1, "ddGKIN_H2O": -21.0, "PhiF_H2O": 0.31, "AUTHOR_KIN": "Friel, C.T., Capaldi, A.P., Radford, S.E.", "REFERENCE_KIN": "Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins. J. Mol. Biol. 326, 293\u2013305. https://doi.org/10.1016/s0022-2836(02)01249-4", "YEAR_KIN": 2003.0, "PMID_KIN": "12547210", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" } ]