[
   {
      "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",
      "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"
      ],
      "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": [
         "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.2004.04.016",
      "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": [
         "E3L"
      ],
      "BACKGROUND_MUT_PDB": [
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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.2004.04.016",
      "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",
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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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      "UniProt": "P32081",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PROTEIN": "CspB Bs (E3L)",
      "SOURCE": "Bacillus subtilis",
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      "UniProt": "P32081",
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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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      "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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      "SOURCE": "Bacillus subtilis",
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      "UniProt": "P32081",
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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",
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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.2004.04.021",
      "YEAR_KIN": 2004.0,
      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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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.2004.04.022",
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      "PMID_KIN": "15147842",
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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.2004.04.022",
      "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",
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      "UniProt": "P32081",
      "PDB_wild": "1csp",
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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",
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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "PMID_KIN": "15147842",
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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",
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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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      "PMID_KIN": "15147842",
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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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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
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      "UniProt": "P32081",
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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",
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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.2004.04.027",
      "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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      "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",
      "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",
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      "UniProt": "P32081",
      "PDB_wild": "1csp",
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      "PFAM": [
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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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      "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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      "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",
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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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      "PMID_KIN": "15147842",
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      "REVIEW_DATE": "2023-06-04T01:00:00"
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      "SOURCE": "Bacillus subtilis",
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]