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Journal of Molecular Biology 383, 224\u2013237. https://doi.org/10.1016/j.jmb.2008.06.081", "YEAR_KIN": 2008.0, "PMID_KIN": "18625240", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "POB (L146A/Y166W)", "SOURCE": "Pyrobaculum aerophilum", "LENGTH": 51.0, "UniProt": "Q8ZUR6", "PDB_wild": "1w4j", "MUTATED_CHAIN": "A", "PFAM": [ "PF02817" ], "CATH": [ "1w4jA00 (4.10.320.10)" ], "EC_NUMBER": "2.3.1.12", "MUTATION_UNIPROT": "WT(L112A,Y132W)", "MUTATION_PDB": "WT(L22A,Y42W)", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump or continuous-flow", "METHOD_KIN": "thermal or GuHCl", "ln(kf)_H2O": 12.25, "ln(ku)_H2O": 6.35, "dGKIN_H2O": 14.64, "mf": -2.93, "mu": 0.71, "BACKGROUND_MUT_UNIPROT": [ "L112A", "Y132W" ], "BACKGROUND_MUT_PDB": [ "WT" ], "AUTHOR_KIN": "Sharpe, T.D., Ferguson, N., Johnson, C.M., Fersht, A.R.", "REFERENCE_KIN": "Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains. Journal of Molecular Biology 383, 224\u2013237. https://doi.org/10.1016/j.jmb.2008.06.081", "YEAR_KIN": 2008.0, "PMID_KIN": "18625240", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "E3BD (F166W)", "SOURCE": "Geobacillus stearothermophilus (Bacillus stearothermophilus)", "LENGTH": 45.0, "UniProt": "P11961", "PDB_wild": "1w4e", "MUTATED_CHAIN": "A", "PFAM": [ "PF02817" ], "CATH": [ "1w4eA00 (4.10.320.10)" ], "EC_NUMBER": "2.3.1.12", "MUTATION_UNIPROT": "WT(F166W)", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.02", "MEASURE_KIN": "T-jump or stopped-flow", "METHOD_KIN": "GuHCl", "ln(kf)_H2O": 10.23, "ln(ku)_H2O": 3.0, "mf": -2.3, "mu": 1.26, "BACKGROUND_MUT_UNIPROT": [ "F166W" ], "AUTHOR_KIN": "Ferguson, N., Sharpe, T.D., Johnson, C.M., Fersht, A.R.", "REFERENCE_KIN": "The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics [WWW Document]. 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Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107", "YEAR_KIN": 2010.0, "PMID_KIN": "20212148", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "Nucleophosmin, Cter-NPM1 domain", "SOURCE": "Homo sapiens", "LENGTH": 52.0, "UniProt": "P06748", "PDB_wild": "2vxd", "MUTATED_CHAIN": "A", "PFAM": [ "PF16276" ], "CATH": [ "2vxdA00 (1.10.10.2100)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.0, "ln(ku)_H2O": 1.06, "dGKIN_H2O": 13.97, "mf": -3.14, "mu": 1.13, "AUTHOR_KIN": "Scaloni F, Federici L, Brunori M, Gianni S", "REFERENCE_KIN": "Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain. Proc Natl Acad Sci U S A.107(12):5447-52. https://doi.org/10.1073/pnas.0910516107", "YEAR_KIN": 2010.0, "PMID_KIN": "20212148", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "FF domain from HYPA/FBP11", "SOURCE": "Homo sapiens", "LENGTH": 70.0, "UniProt": "O75400", "PDB_wild": "1uzc", "MUTATED_CHAIN": "A", "PFAM": [ "PF01846" ], "CATH": [ "1uzcA00 (1.10.10.440)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 5.7, "BUFFER_NAME": "Na-Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.7, "ln(ku)_H2O": 1.3, "dGKIN_H2O": 15.23, "mf": -4.23, "mu": -0.64, "AUTHOR_KIN": "Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR", "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067", "YEAR_KIN": 2005.0, "PMID_KIN": "15935381", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "FF domain from HYPA/FBP11", "SOURCE": "Homo sapiens", "LENGTH": 70.0, "UniProt": "O75400", "PDB_wild": "1uzc", "MUTATED_CHAIN": "A", "PFAM": [ "PF01846" ], "CATH": [ "1uzcA00 (1.10.10.440)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 5.7, "BUFFER_NAME": "Na-Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.7, "ln(ku)_H2O": 1.3, "dGKIN_H2O": 15.23, "mf": -4.23, "mu": -0.64, "AUTHOR_KIN": "Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR", "REFERENCE_KIN": "The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol. 350(2):363-78. https://doi.org/10.1016/j.jmb.2005.04.067", "YEAR_KIN": 2005.0, "PMID_KIN": "15935381", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "Grb2-SH3", "SOURCE": "Homo sapiens", "LENGTH": 56.0, "UniProt": "P62993", "PDB_wild": "2vwf", "MUTATED_CHAIN": "A", "PFAM": [ "PF00018" ], "CATH": [ "2vwfA00 (2.30.30.40)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 22.0, "pH": 7.2, "BUFFER_NAME": "NaPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 2.77, "ln(ku)_H2O": -1.97, "dGKIN_H2O": 11.74, "mf": -2.47, "mu": 0.59, "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S", "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320", "YEAR_KIN": 2018.0, "PMID_KIN": "30091591", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "Grb2-SH3", "SOURCE": "Homo sapiens", "LENGTH": 56.0, "UniProt": "P62993", "PDB_wild": "2vwf", "MUTATED_CHAIN": "A", "PFAM": [ "PF00018" ], "CATH": [ "2vwfA00 (2.30.30.40)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 22.0, "pH": 7.2, "BUFFER_NAME": "NaPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 2.77, "ln(ku)_H2O": -1.97, "dGKIN_H2O": 11.74, "mf": -2.47, "mu": 0.59, "AUTHOR_KIN": "Troilo F, Bonetti D, Camilloni C, Toto A, Longhi S, Brunori M, Gianni S", "REFERENCE_KIN": "Folding Mechanism of the SH3 Domain from Grb2. J Phys Chem B 122(49):11166-11173. https://doi.org/10.1021/acs.jpcb.8b06320", "YEAR_KIN": 2018.0, "PMID_KIN": "30091591", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "BBL domain (H142W)", "SOURCE": "Escherichia coli", "LENGTH": 45.0, "UniProt": "P0AFG6", "PDB_wild": "2wxc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02817" ], "CATH": [ "2wxcA00 (4.10.320.10)" ], "EC_NUMBER": "2.3.1.61", "MUTATION_UNIPROT": "WT(H125W)", "MUTATION_PDB": "WT(H142W)", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 11.17, "ln(ku)_H2O": 6.65, "dGKIN_H2O": 10.67, "mf": -2.34, "mu": 0.54, "BACKGROUND_MUT_UNIPROT": [ "H125W" ], "BACKGROUND_MUT_PDB": [ "H142W" ], "AUTHOR_KIN": "Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR", "REFERENCE_KIN": "The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011", "YEAR_KIN": 2009.0, "PMID_KIN": "19445954", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "BBL domain (H142W)", "SOURCE": "Escherichia coli", "LENGTH": 45.0, "UniProt": "P0AFG6", "PDB_wild": "2wxc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02817" ], "CATH": [ "2wxcA00 (4.10.320.10)" ], "EC_NUMBER": "2.3.1.61", "MUTATION_UNIPROT": "WT(H125W)", "MUTATION_PDB": "WT(H142W)", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 11.17, "ln(ku)_H2O": 6.65, "dGKIN_H2O": 10.67, "mf": -2.34, "mu": 0.54, "BACKGROUND_MUT_UNIPROT": [ "H125W" ], "BACKGROUND_MUT_PDB": [ "H142W" ], "AUTHOR_KIN": "Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR", "REFERENCE_KIN": "The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011", "YEAR_KIN": 2009.0, "PMID_KIN": "19445954", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "BBL domain (L131W)", "SOURCE": "Escherichia coli", "LENGTH": 45.0, "UniProt": "P0AFG6", "PDB_wild": "2wxc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02817" ], "CATH": [ "2wxcA00 (4.10.320.10)" ], "EC_NUMBER": "2.3.1.61", "MUTATION_UNIPROT": "WT(L114W)", "MUTATION_PDB": "WT(L131W)", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 10.4, "ln(ku)_H2O": 6.46, "dGKIN_H2O": 9.29, "mf": -2.18, "mu": 0.71, "BACKGROUND_MUT_UNIPROT": [ "L114W" ], "BACKGROUND_MUT_PDB": [ "L131W" ], "AUTHOR_KIN": "Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR", "REFERENCE_KIN": "The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011", "YEAR_KIN": 2009.0, "PMID_KIN": "19445954", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "BBL domain (L131W)", "SOURCE": "Escherichia coli", "LENGTH": 45.0, "UniProt": "P0AFG6", "PDB_wild": "2wxc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02817" ], "CATH": [ "2wxcA00 (4.10.320.10)" ], "EC_NUMBER": "2.3.1.61", "MUTATION_UNIPROT": "WT(L114W)", "MUTATION_PDB": "WT(L131W)", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 10.4, "ln(ku)_H2O": 6.46, "dGKIN_H2O": 9.29, "mf": -2.18, "mu": 0.71, "BACKGROUND_MUT_UNIPROT": [ "L114W" ], "BACKGROUND_MUT_PDB": [ "L131W" ], "AUTHOR_KIN": "Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR", "REFERENCE_KIN": "The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. J Mol Biol.390(5):1060-73. https://doi.org/10.1016/j.jmb.2009.05.011", "YEAR_KIN": 2009.0, "PMID_KIN": "19445954", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "RIBOSOMAL PROTEIN S6", "SOURCE": "Thermus thermophylus", "LENGTH": 101.0, "UniProt": "P23370", "PDB_wild": "1ris", "MUTATED_CHAIN": "A", "PFAM": [ "PF01250" ], "CATH": [ "1risA00 (3.30.70.60)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 6.3, "BUFFER_NAME": "MES", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 5.83, "ln(ku)_H2O": -8.59, "dGKIN_H2O": 35.56, "mf": -5.06, "mu": 2.47, "CM_KIN": 3.47, "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M", "REFERENCE_KIN": "Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016", "YEAR_KIN": 2007.0, "PMID_KIN": "17056063", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "RIBOSOMAL PROTEIN S6", "SOURCE": "Thermus thermophylus", "LENGTH": 101.0, "UniProt": "P23370", "PDB_wild": "1ris", "MUTATED_CHAIN": "A", "PFAM": [ "PF01250" ], "CATH": [ "1risA00 (3.30.70.60)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 6.3, "BUFFER_NAME": "MES", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 5.83, "ln(ku)_H2O": -8.59, "dGKIN_H2O": 35.56, "mf": -5.06, "mu": 2.47, "CM_KIN": 3.47, "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M", "REFERENCE_KIN": "Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016", "YEAR_KIN": 2007.0, "PMID_KIN": "17056063", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "30S ribosomal protein S6", "SOURCE": "Aquifex aeolicus", "LENGTH": 110.0, "UniProt": "O66474", "PDB_wild": "2j5a", "MUTATED_CHAIN": "A", "PFAM": [ "PF01250" ], "CATH": [ "2j5aA00 (3.30.70.60)" ], "MUTATION_UNIPROT": "WT(W95F)", "MUTATION_PDB": "WT(W95F)", "T": 25.0, "pH": 6.3, "BUFFER_NAME": "MES", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 7.32, "ln(ku)_H2O": -10.92, "dGKIN_H2O": 45.1, "mf": -6.32, "mu": 2.26, "CM_KIN": 3.86, "BACKGROUND_MUT_UNIPROT": [ "W95F" ], "BACKGROUND_MUT_PDB": [ "W95F" ], "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M", "REFERENCE_KIN": "Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016", "YEAR_KIN": 2007.0, "PMID_KIN": "17056063", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "30S ribosomal protein S6", "SOURCE": "Aquifex aeolicus", "LENGTH": 110.0, "UniProt": "O66474", "PDB_wild": "2j5a", "MUTATED_CHAIN": "A", "PFAM": [ "PF01250" ], "CATH": [ "2j5aA00 (3.30.70.60)" ], "MUTATION_UNIPROT": "WT(W95F)", "MUTATION_PDB": "WT(W95F)", "T": 25.0, "pH": 6.3, "BUFFER_NAME": "MES", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 7.32, "ln(ku)_H2O": -10.92, "dGKIN_H2O": 45.1, "mf": -6.32, "mu": 2.26, "CM_KIN": 3.86, "BACKGROUND_MUT_UNIPROT": [ "W95F" ], "BACKGROUND_MUT_PDB": [ "W95F" ], "AUTHOR_KIN": "Olofsson M, Hansson S, Hedberg L, Logan DT, Oliveberg M", "REFERENCE_KIN": "Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons. J Mol Biol. 365(1):237-48. https://doi.org/10.1016/j.jmb.2006.09.016", "YEAR_KIN": 2007.0, "PMID_KIN": "17056063", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "CKS1", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P61024", "PDB_wild": "1dkt", "MUTATED_CHAIN": "A", "PFAM": [ "PF01111" ], "CATH": [ "1dktA00 (3.30.170.10)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.5, "BUFFER_NAME": "Tris-HCl", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 4.52, "ln(ku)_H2O": -2.73, "dGKIN_H2O": 16.99, "mf": -1.44, "mu": 3.22, "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS", "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0", "YEAR_KIN": 2003.0, "PMID_KIN": "12473461", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "CKS1", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P61024", "PDB_wild": "1dkt", "MUTATED_CHAIN": "A", "PFAM": [ "PF01111" ], "CATH": [ "1dktA00 (3.30.170.10)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.5, "BUFFER_NAME": "Tris-HCl", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM EDTA", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 4.52, "ln(ku)_H2O": -2.73, "dGKIN_H2O": 16.99, "mf": -1.44, "mu": 3.22, "AUTHOR_KIN": "Seeliger MA, Breward SE, Itzhaki LS", "REFERENCE_KIN": "Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family. J Mol Biol. 325(1):189-99. https://doi.org/10.1016/s0022-2836(02)01202-0", "YEAR_KIN": 2003.0, "PMID_KIN": "12473461", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "SAP (L31W) domain of THO1", "SOURCE": "Saccharomyces cerevisiae", "LENGTH": 49.0, "UniProt": "P40040", "PDB_wild": "2wqg", "MUTATED_CHAIN": "A", "PFAM": [ "PF02037" ], "CATH": [ "2wqgA00 (1.10.720.30)" ], "MUTATION_UNIPROT": "WT(L30W)", "MUTATION_PDB": "WT(L31W)", "T": 10.0, "pH": 6.0, "BUFFER_NAME": "MES", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 8.06, "ln(ku)_H2O": 2.08, "dGKIN_H2O": 14.07, "mf": -1.76, "mu": 0.88, "CM_KIN": -2.64, "AUTHOR_KIN": "Dodson CA, Arbely E", "REFERENCE_KIN": "Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002", "YEAR_KIN": 2015.0, "PMID_KIN": "26073259", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "SAP (L31W) domain of THO1", "SOURCE": "Saccharomyces cerevisiae", "LENGTH": 49.0, "UniProt": "P40040", "PDB_wild": "2wqg", "MUTATED_CHAIN": "A", "PFAM": [ "PF02037" ], "CATH": [ "2wqgA00 (1.10.720.30)" ], "MUTATION_UNIPROT": "WT(L30W)", "MUTATION_PDB": "WT(L31W)", "T": 10.0, "pH": 6.0, "BUFFER_NAME": "MES", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 8.06, "ln(ku)_H2O": 2.08, "dGKIN_H2O": 14.07, "mf": -1.76, "mu": 0.88, "CM_KIN": -2.64, "AUTHOR_KIN": "Dodson CA, Arbely E", "REFERENCE_KIN": "Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett. 589(15):1740-7. https://doi.org/10.1016/j.febslet.2015.06.002", "YEAR_KIN": 2015.0, "PMID_KIN": "26073259", "STATE": "Yes", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "Rd-apocyt b562 (de novo)", "SOURCE": "Escherichia coli", "LENGTH": 106.0, "UniProt": "P0ABE7", "PDB_wild": "1yyj", "MUTATED_CHAIN": "A", "MUTATION_UNIPROT": "WT(M7W,R98I,N99R,H102N,R106G)", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.0, "BUFFER_NAME": "NaAcetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.02, "ln(ku)_H2O": -3.91, "dGKIN_H2O": 22.12, "mf": -3.35, "mu": 3.68, "BACKGROUND_MUT_UNIPROT": [ "M7W", "R98I", "N99R", "H102N", "R106G" ], "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.", "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n", "YEAR_KIN": 2002.0, "PMID_KIN": "12069590", "STATE": "2", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "Rd-apocyt b562 (de novo)", "SOURCE": "Escherichia coli", "LENGTH": 106.0, "UniProt": "P0ABE7", "PDB_wild": "1yyj", "MUTATED_CHAIN": "A", "MUTATION_UNIPROT": "WT(M7W,R98I,N99R,H102N,R106G)", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.0, "BUFFER_NAME": "NaAcetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.02, "ln(ku)_H2O": -3.91, "dGKIN_H2O": 22.12, "mf": -3.35, "mu": 3.68, "BACKGROUND_MUT_UNIPROT": [ "M7W", "R98I", "N99R", "H102N", "R106G" ], "AUTHOR_KIN": "Chu R, Pei W, Takei J, Bai Y.", "REFERENCE_KIN": "Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry. 41(25):7998-8003. doi: 10.1021/bi025872n", "YEAR_KIN": 2002.0, "PMID_KIN": "12069590", "STATE": "2", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "BdpA (Y17W)", "SOURCE": "Staphylococcus aureus", "LENGTH": 62.0, "UniProt": "P38507", "PDB_wild": "1ss1", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1ss1A00 (1.20.5.420)" ], "MUTATION_UNIPROT": "WT(Y225W)", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal", "ln(kf)_H2O": 11.48, "ln(ku)_H2O": 3.22, "dGKIN_H2O": 20.5, "mf": -4.81, "mu": 1.0, "BACKGROUND_MUT_UNIPROT": [ "Y225W" ], "BACKGROUND_MUT_PDB": [ "WT" ], "AUTHOR_KIN": "Sato, S., Fersht, A.R.", "REFERENCE_KIN": "Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254\u2013267. https://doi.org/10.1016/j.jmb.2007.06.043", "YEAR_KIN": 2007.0, "PMID_KIN": "17628591", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "BdpA (Y17W)", "SOURCE": "Staphylococcus aureus", "LENGTH": 62.0, "UniProt": "P38507", "PDB_wild": "1ss1", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1ss1A00 (1.20.5.420)" ], "MUTATION_UNIPROT": "WT(Y225W)", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal", "ln(kf)_H2O": 11.48, "ln(ku)_H2O": 3.22, "dGKIN_H2O": 20.5, "mf": -4.81, "mu": 1.0, "BACKGROUND_MUT_UNIPROT": [ "Y225W" ], "BACKGROUND_MUT_PDB": [ "WT" ], "AUTHOR_KIN": "Sato, S., Fersht, A.R.", "REFERENCE_KIN": "Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254\u2013267. https://doi.org/10.1016/j.jmb.2007.06.043", "YEAR_KIN": 2007.0, "PMID_KIN": "17628591", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "Cold shock protein CspB", "SOURCE": "Bacillus caldolyticus", "LENGTH": 66.0, "UniProt": "P41016", "PDB_wild": "1c9o", "MUTATED_CHAIN": "A", "PFAM": [ "PF00313" ], "CATH": [ "1c9oA00 (2.40.50.140)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Na cacodylate-HCI", "BUFFER_CONC": "0.1", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 7.22, "ln(ku)_H2O": -0.45, "dGKIN_H2O": 19.0, "AUTHOR_KIN": "Perl D, Welker C, Schindler T, Schr\u00f6der K, Marahiel MA, Jaenicke R, Schmid FX", "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229", "YEAR_KIN": 1998.0, "PMID_KIN": "9501917", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Cold shock protein CspB", "SOURCE": "Bacillus caldolyticus", "LENGTH": 66.0, "UniProt": "P41016", "PDB_wild": "1c9o", "MUTATED_CHAIN": "A", "PFAM": [ "PF00313" ], "CATH": [ "1c9oA00 (2.40.50.140)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Na cacodylate-HCI", "BUFFER_CONC": "0.1", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 7.22, "ln(ku)_H2O": -0.45, "dGKIN_H2O": 19.0, "AUTHOR_KIN": "Perl D, Welker C, Schindler T, Schr\u00f6der K, Marahiel MA, Jaenicke R, Schmid FX", "REFERENCE_KIN": "Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229", "YEAR_KIN": 1998.0, "PMID_KIN": "9501917", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D", "SOURCE": "Escherichia coli", "LENGTH": 48.0, "UniProt": "P0AEZ7", "PDB_wild": "1e0g", "MUTATED_CHAIN": "A", "PFAM": [ "PF01476" ], "CATH": [ "1e0gA00 (3.10.350.10)" ], "EC_NUMBER": "4.2.2.n1", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 11.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "dGKIN_H2O": 12.13, "mu": 5.02, "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J", "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020", "YEAR_KIN": 2008.0, "PMID_KIN": "18538343", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "LysM domain of Membrane-bound lytic murein transglycosylase D", "SOURCE": "Escherichia coli", "LENGTH": 48.0, "UniProt": "P0AEZ7", "PDB_wild": "1e0g", "MUTATED_CHAIN": "A", "PFAM": [ "PF01476" ], "CATH": [ "1e0gA00 (3.10.350.10)" ], "EC_NUMBER": "4.2.2.n1", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 11.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "dGKIN_H2O": 12.13, "mu": 5.02, "AUTHOR_KIN": "Nickson AA, Stoll KE, Clarke J", "REFERENCE_KIN": "Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder. J Mol Bio 380(3):557-69. https://doi.org/10.1016/j.jmb.2008.05.020", "YEAR_KIN": 2008.0, "PMID_KIN": "18538343", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "FADD-DD Fas-associated death domain protein", "SOURCE": "Homo sapiens", "LENGTH": 100.0, "UniProt": "Q13158", "PDB_wild": "1e41", "MUTATED_CHAIN": "A", "PFAM": [ "PF00531" ], "CATH": [ "1e41A00 (1.10.533.10)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "5 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "Urea", "mu": 5.86, "beta-T": 0.76, "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J", "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol. 389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004", "YEAR_KIN": 2009.0, "PMID_KIN": "19362094", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "FADD-DD Fas-associated death domain protein", "SOURCE": "Homo sapiens", "LENGTH": 100.0, "UniProt": "Q13158", "PDB_wild": "1e41", "MUTATED_CHAIN": "A", "PFAM": [ "PF00531" ], "CATH": [ "1e41A00 (1.10.533.10)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "5 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "Urea", "mu": 5.86, "beta-T": 0.76, "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J", "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol. 389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004", "YEAR_KIN": 2009.0, "PMID_KIN": "19362094", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "NTL9", "SOURCE": "Geobacillus stearothermophilus", "LENGTH": 56.0, "UniProt": "P02417", "PDB_wild": "2hbb", "MUTATED_CHAIN": "A", "PFAM": [ "PF01281" ], "CATH": [ "2hbbA00 (3.40.5.10)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.45, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.02", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GuHCl", "ln(kf)_H2O": 6.76, "ln(ku)_H2O": -0.11, "dGKIN_H2O": 17.02, "mf": -1.88, "mu": 0.84, "AUTHOR_KIN": "Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP", "REFERENCE_KIN": "The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034", "YEAR_KIN": 2017.0, "PMID_KIN": "28494951", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "NTL9", "SOURCE": "Geobacillus stearothermophilus", "LENGTH": 56.0, "UniProt": "P02417", "PDB_wild": "2hbb", "MUTATED_CHAIN": "A", "PFAM": [ "PF01281" ], "CATH": [ "2hbbA00 (3.40.5.10)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.45, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.02", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GuHCl", "ln(kf)_H2O": 6.76, "ln(ku)_H2O": -0.11, "dGKIN_H2O": 17.02, "mf": -1.88, "mu": 0.84, "AUTHOR_KIN": "Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP", "REFERENCE_KIN": "The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State, Biophys J, 112(9):1797-1806. https://doi.org/10.1016/j.bpj.2017.01.034", "YEAR_KIN": 2017.0, "PMID_KIN": "28494951", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "PSD1(D27E/Y28K/E43W)", "SOURCE": "Finegoldia magna", "LENGTH": 50.0, "UniProt": "Q51918", "PDB_wild": "2fs1", "MUTATED_CHAIN": "A", "PFAM": [ "PF17573" ], "CATH": [ "2fs1A00 (1.10.8.40)" ], "MUTATION_PDB": "WT(D17E,Y28K,E43W)", "T": 25.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow or T-Jump Fluorescence Sectroscopy", "METHOD_KIN": "GndHCl", "ln(kf)_H2O": 8.96, "ln(ku)_H2O": 0.88, "dGKIN_H2O": 20.02, "BACKGROUND_MUT_PDB": [ "D17E", "Y28K", "E43W" ], "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.", "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109", "YEAR_KIN": 2012.0, "PMID_KIN": "22652570", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "PSD1(D27E/Y28K/E43W)", "SOURCE": "Finegoldia magna", "LENGTH": 50.0, "UniProt": "Q51918", "PDB_wild": "2fs1", "MUTATED_CHAIN": "A", "PFAM": [ "PF17573" ], "CATH": [ "2fs1A00 (1.10.8.40)" ], "MUTATION_PDB": "WT(D17E,Y28K,E43W)", "T": 25.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow or T-Jump Fluorescence Sectroscopy", "METHOD_KIN": "GndHCl", "ln(kf)_H2O": 8.96, "ln(ku)_H2O": 0.88, "dGKIN_H2O": 20.02, "BACKGROUND_MUT_PDB": [ "D17E", "Y28K", "E43W" ], "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.", "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109", "YEAR_KIN": 2012.0, "PMID_KIN": "22652570", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "PSD1(Ga77 mutant)", "SOURCE": "Finegoldia magna", "LENGTH": 50.0, "PDB_wild": "2jws", "MUTATED_CHAIN": "A", "MUTATION_PDB": "WT(T51K,F52A)", "T": 10.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow, or T-Jump Fluorescence Sectroscopy", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.81, "ln(ku)_H2O": 1.34, "dGKIN_H2O": 16.03, "BACKGROUND_MUT_PDB": [ "T51K", "F52A" ], "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.", "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109", "YEAR_KIN": 2012.0, "PMID_KIN": "22652570", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "PSD1(Ga77 mutant)", "SOURCE": "Finegoldia magna", "LENGTH": 50.0, "PDB_wild": "2jws", "MUTATED_CHAIN": "A", "MUTATION_PDB": "WT(T51K,F52A)", "T": 10.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow, or T-Jump Fluorescence Sectroscopy", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.81, "ln(ku)_H2O": 1.34, "dGKIN_H2O": 16.03, "BACKGROUND_MUT_PDB": [ "T51K", "F52A" ], "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.", "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109", "YEAR_KIN": 2012.0, "PMID_KIN": "22652570", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "PSD1(Ga88 mutant)", "SOURCE": "Finegoldia magna", "LENGTH": 50.0, "PDB_wild": "2jws", "MUTATED_CHAIN": "A", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow, or T-Jump Fluorescence Sectroscopy", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.31, "ln(ku)_H2O": 1.86, "dGKIN_H2O": 13.5, "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.", "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. Proc Natl Acad Sci U S A 109(44):17772-6. https://doi.org/10.1073/pnas.1201794109", "YEAR_KIN": 2012.0, "PMID_KIN": "22652570", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "PSD1(Ga88 mutant)", "SOURCE": "Finegoldia magna", "LENGTH": 50.0, "PDB_wild": "2jws", "MUTATED_CHAIN": "A", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow, or T-Jump Fluorescence Sectroscopy", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.31, "ln(ku)_H2O": 1.86, "dGKIN_H2O": 13.5, "AUTHOR_KIN": "Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.", "REFERENCE_KIN": "Folding pathways of proteins with increasing degree of sequence identities but different structure and function. 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Nature. 1997 390(6656):196-9. https://doi.org/10.1038/36626", "YEAR_KIN": 1997.0, "PMID_KIN": "9367160", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "ADAh2", "SOURCE": "Homo sapiens", "LENGTH": 81.0, "UniProt": "P48052", "PDB_wild": "1o6x", "MUTATED_CHAIN": "A", "PFAM": [ "PF02244" ], "CATH": [ "1o6xA00 (3.30.70.340)" ], "EC_NUMBER": "3.4.17.15", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.63, "ln(ku)_H2O": -0.73, "dGKIN_H2O": 18.41, "mf": -2.93, "mu": 1.21, "AUTHOR_KIN": "Villegas, V., Mart\u00ednez, J.C., Avil\u00e9s, F.X., Serrano, L.", "REFERENCE_KIN": "Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. 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Nat Struct Biol. 229-35. https://doi.org/10.1038/nsb0398-229", "YEAR_KIN": 1998.0, "PMID_KIN": "9501917", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "B-domain of staphylococcal proteinA", "SOURCE": "Staphylococcus aureus", "LENGTH": 58.0, "UniProt": "P38507", "PDB_wild": "1bdc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1bdcA00 (1.20.5.420)" ], "MUTATION_PDB": "WT", "T": 37.0, "pH": 5.0, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.02", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 11.7, "ln(ku)_H2O": 4.22, "dGKIN_H2O": 19.28, "AUTHOR_KIN": "Myers JK, Oas TG", "REFERENCE_KIN": "Preorganized secondary structure as an important determinant of fast protein folding. Nat Struct Biol. 2001 8(6):552-8", "YEAR_KIN": 2001.0, "PMID_KIN": "11373626", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "B-domain of staphylococcal proteinA", "SOURCE": "Staphylococcus aureus", "LENGTH": 58.0, "UniProt": "P38507", "PDB_wild": "1bdc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1bdcA00 (1.20.5.420)" ], "MUTATION_PDB": "WT", "T": 37.0, "pH": 5.0, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.02", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 11.7, "ln(ku)_H2O": 4.22, "dGKIN_H2O": 19.28, "AUTHOR_KIN": "Myers JK, Oas TG", "REFERENCE_KIN": "Preorganized secondary structure as an important determinant of fast protein folding. Nat Struct Biol. 2001 8(6):552-8", "YEAR_KIN": 2001.0, "PMID_KIN": "11373626", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "BdpA (N31H/Q35W)", "SOURCE": "Staphylococcus aureus", "LENGTH": 60.0, "UniProt": "P38507", "PDB_wild": "1bdc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1bdcA00 (1.20.5.420)" ], "MUTATION_UNIPROT": "WT(N239H,Q243W)", "MUTATION_PDB": "WT(N29H,Q33W)", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal", "ln(kf)_H2O": 8.77, "ln(ku)_H2O": 2.13, "dGKIN_H2O": 16.44, "ddGKIN_H2O": -4.06, "mf": -4.18, "mu": 1.88, "BACKGROUND_MUT_UNIPROT": [ "N239H", "Q243W" ], "BACKGROUND_MUT_PDB": [ "N29H", "Q33W" ], "AUTHOR_KIN": "Sato, S., Fersht, A.R.", "REFERENCE_KIN": "Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254\u2013267. https://doi.org/10.1016/j.jmb.2007.06.043", "YEAR_KIN": 2007.0, "PMID_KIN": "17628591", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "BdpA (N31H/Q35W)", "SOURCE": "Staphylococcus aureus", "LENGTH": 60.0, "UniProt": "P38507", "PDB_wild": "1bdc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1bdcA00 (1.20.5.420)" ], "MUTATION_UNIPROT": "WT(N239H,Q243W)", "MUTATION_PDB": "WT(N29H,Q33W)", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal", "ln(kf)_H2O": 8.77, "ln(ku)_H2O": 2.13, "dGKIN_H2O": 16.44, "ddGKIN_H2O": -4.06, "mf": -4.18, "mu": 1.88, "BACKGROUND_MUT_UNIPROT": [ "N239H", "Q243W" ], "BACKGROUND_MUT_PDB": [ "N29H", "Q33W" ], "AUTHOR_KIN": "Sato, S., Fersht, A.R.", "REFERENCE_KIN": "Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254\u2013267. https://doi.org/10.1016/j.jmb.2007.06.043", "YEAR_KIN": 2007.0, "PMID_KIN": "17628591", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "BdpA (E50W)", "SOURCE": "Staphylococcus aureus", "LENGTH": 60.0, "UniProt": "P38507", "PDB_wild": "1bdc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1bdcA00 (1.20.5.420)" ], "MUTATION_UNIPROT": "WT(E258W)", "MUTATION_PDB": "WT(E48W)", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal", "ln(kf)_H2O": 11.29, "ln(ku)_H2O": 3.44, "dGKIN_H2O": 19.46, "ddGKIN_H2O": -1.04, "mf": -4.69, "mu": 1.72, "BACKGROUND_MUT_UNIPROT": [ "E258W" ], "BACKGROUND_MUT_PDB": [ "E48W" ], "AUTHOR_KIN": "Sato, S., Fersht, A.R.", "REFERENCE_KIN": "Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254\u2013267. https://doi.org/10.1016/j.jmb.2007.06.043", "YEAR_KIN": 2007.0, "PMID_KIN": "17628591", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "BdpA (E50W)", "SOURCE": "Staphylococcus aureus", "LENGTH": 60.0, "UniProt": "P38507", "PDB_wild": "1bdc", "MUTATED_CHAIN": "A", "PFAM": [ "PF02216" ], "CATH": [ "1bdcA00 (1.20.5.420)" ], "MUTATION_UNIPROT": "WT(E258W)", "MUTATION_PDB": "WT(E48W)", "T": 25.0, "pH": 5.5, "BUFFER_NAME": "Sodium Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal", "ln(kf)_H2O": 11.29, "ln(ku)_H2O": 3.44, "dGKIN_H2O": 19.46, "ddGKIN_H2O": -1.04, "mf": -4.69, "mu": 1.72, "BACKGROUND_MUT_UNIPROT": [ "E258W" ], "BACKGROUND_MUT_PDB": [ "E48W" ], "AUTHOR_KIN": "Sato, S., Fersht, A.R.", "REFERENCE_KIN": "Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A. J. Mol. Biol. 372, 254\u2013267. https://doi.org/10.1016/j.jmb.2007.06.043", "YEAR_KIN": 2007.0, "PMID_KIN": "17628591", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "Cold shock protein CspA", "SOURCE": "Escherichia coli (strain K12)", "LENGTH": 69.0, "UniProt": "P0A9X9", "PDB_wild": "1mjc", "MUTATED_CHAIN": "A", "PFAM": [ "PF00313" ], "CATH": [ "1mjcA00 (2.40.50.140)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.29, "ln(ku)_H2O": 1.44, "dGKIN_H2O": 9.54, "AUTHOR_KIN": "Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM", "REFERENCE_KIN": "Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7(2):470-9", "YEAR_KIN": 1998.0, "PMID_KIN": "9521124", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Cold shock protein CspA", "SOURCE": "Escherichia coli (strain K12)", "LENGTH": 69.0, "UniProt": "P0A9X9", "PDB_wild": "1mjc", "MUTATED_CHAIN": "A", "PFAM": [ "PF00313" ], "CATH": [ "1mjcA00 (2.40.50.140)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.29, "ln(ku)_H2O": 1.44, "dGKIN_H2O": 9.54, "AUTHOR_KIN": "Reid KL, Rodriguez HM, Hillier BJ, Gregoret LM", "REFERENCE_KIN": "Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA. Protein Sci. 7(2):470-9", "YEAR_KIN": 1998.0, "PMID_KIN": "9521124", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Phosphocarrier protein HPr", "SOURCE": "Escherichia coli (strain K12)", "LENGTH": 85.0, "UniProt": "P0AA04", "PDB_wild": "1opd", "MUTATED_CHAIN": "A", "PFAM": [ "PF00381" ], "CATH": [ "1opdA00 (3.30.1340.10)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.1", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdnHCl", "ln(kf)_H2O": 2.7, "ln(ku)_H2O": -6.17, "dGKIN_H2O": 21.61, "AUTHOR_KIN": "Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM", "REFERENCE_KIN": "Slow cooperative folding of a small globular protein HPr. Biochemistry. 37(2):622-37", "YEAR_KIN": 1998.0, "PMID_KIN": "9425085", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Phosphocarrier protein HPr", "SOURCE": "Escherichia coli (strain K12)", "LENGTH": 85.0, "UniProt": "P0AA04", "PDB_wild": "1opd", "MUTATED_CHAIN": "A", "PFAM": [ "PF00381" ], "CATH": [ "1opdA00 (3.30.1340.10)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.1", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdnHCl", "ln(kf)_H2O": 2.7, "ln(ku)_H2O": -6.17, "dGKIN_H2O": 21.61, "AUTHOR_KIN": "Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM", "REFERENCE_KIN": "Slow cooperative folding of a small globular protein HPr. Biochemistry. 37(2):622-37", "YEAR_KIN": 1998.0, "PMID_KIN": "9425085", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "TRF1 Myb domain (Telomeric repeat-binding factor 1)", "SOURCE": "Homo sapiens", "LENGTH": 53.0, "UniProt": "P54274", "PDB_wild": "1ba5", "MUTATED_CHAIN": "A", "PFAM": [ "PF00249" ], "CATH": [ "1ba5A00 (1.10.10.60)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.7, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.91, "ln(ku)_H2O": 1.16, "dGKIN_H2O": 11.8, "mf": -3.6, "mu": 0.38, "beta-T": 0.9, "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR", "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100", "YEAR_KIN": 2003.0, "PMID_KIN": "14595026", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "TRF1 Myb domain (Telomeric repeat-binding factor 1)", "SOURCE": "Homo sapiens", "LENGTH": 53.0, "UniProt": "P54274", "PDB_wild": "1ba5", "MUTATED_CHAIN": "A", "PFAM": [ "PF00249" ], "CATH": [ "1ba5A00 (1.10.10.60)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.7, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.91, "ln(ku)_H2O": 1.16, "dGKIN_H2O": 11.8, "mf": -3.6, "mu": 0.38, "beta-T": 0.9, "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR", "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100", "YEAR_KIN": 2003.0, "PMID_KIN": "14595026", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "RAP1 Myb domain (Telomeric repeat-binding factor 2-interacting protein 1)", "SOURCE": "Homo sapiens", "LENGTH": 59.0, "UniProt": "Q9NYB0", "PDB_wild": "1fex", "MUTATED_CHAIN": "A", "PFAM": [ "PF08914" ], "CATH": [ "1fexA00 (1.10.10.60)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.7, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.73, "ln(ku)_H2O": 2.89, "dGKIN_H2O": 13.05, "mf": -2.85, "mu": 0.63, "beta-T": 0.82, "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR", "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100", "YEAR_KIN": 2003.0, "PMID_KIN": "14595026", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "RAP1 Myb domain (Telomeric repeat-binding factor 2-interacting protein 1)", "SOURCE": "Homo sapiens", "LENGTH": 59.0, "UniProt": "Q9NYB0", "PDB_wild": "1fex", "MUTATED_CHAIN": "A", "PFAM": [ "PF08914" ], "CATH": [ "1fexA00 (1.10.10.60)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 5.7, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.73, "ln(ku)_H2O": 2.89, "dGKIN_H2O": 13.05, "mf": -2.85, "mu": 0.63, "beta-T": 0.82, "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR", "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100", "YEAR_KIN": 2003.0, "PMID_KIN": "14595026", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "c-Myb-transforming protein (Transcriptional activator Myb)", "SOURCE": "Mus musculus", "LENGTH": 53.0, "UniProt": "P06876", "PDB_wild": "1idy", "MUTATED_CHAIN": "A", "PFAM": [ "PF00249" ], "CATH": [ "1idyA00 (1.10.10.60)" ], "MUTATION_PDB": "WT(I155L)", "T": 25.0, "pH": 5.7, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.19, "ln(ku)_H2O": 1.67, "dGKIN_H2O": 17.45, "mf": -2.72, "mu": 0.71, "beta-T": 0.79, "BACKGROUND_MUT_PDB": [ "I155L" ], "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR", "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100", "YEAR_KIN": 2003.0, "PMID_KIN": "14595026", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "c-Myb-transforming protein (Transcriptional activator Myb)", "SOURCE": "Mus musculus", "LENGTH": 53.0, "UniProt": "P06876", "PDB_wild": "1idy", "MUTATED_CHAIN": "A", "PFAM": [ "PF00249" ], "CATH": [ "1idyA00 (1.10.10.60)" ], "MUTATION_PDB": "WT(I155L)", "T": 25.0, "pH": 5.7, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.19, "ln(ku)_H2O": 1.67, "dGKIN_H2O": 17.45, "mf": -2.72, "mu": 0.71, "beta-T": 0.79, "BACKGROUND_MUT_PDB": [ "I155L" ], "AUTHOR_KIN": "Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR", "REFERENCE_KIN": "Unifying features in protein-folding mechanisms. Proc Natl Acad Sci U S A. 100(23):13286-91. https://doi.org/10.1073/pnas.1835776100", "YEAR_KIN": 2003.0, "PMID_KIN": "14595026", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Yes kinase-associated protein (Transcriptional coactivator YAP1)", "SOURCE": "Homo sapiens", "LENGTH": 45.0, "UniProt": "P46937", "PDB_wild": "1jmq", "MUTATED_CHAIN": "A", "PFAM": [ "PF00397" ], "CATH": [ "1jmqA00 (2.20.70.10)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "NaPi", "BUFFER_CONC": "0.02", "MEASURE_KIN": "continuous-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.4, "ln(ku)_H2O": 6.7, "dGKIN_H2O": 4.24, "AUTHOR_KIN": "Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.", "REFERENCE_KIN": "Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. Proc. Natl. Acad. Sci. U.S.A. 98, 13002\u201313007. https://doi.org/10.1073/pnas.221467198", "YEAR_KIN": 2001.0, "PMID_KIN": "11687613", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Yes kinase-associated protein (Transcriptional coactivator YAP1)", "SOURCE": "Homo sapiens", "LENGTH": 45.0, "UniProt": "P46937", "PDB_wild": "1jmq", "MUTATED_CHAIN": "A", "PFAM": [ "PF00397" ], "CATH": [ "1jmqA00 (2.20.70.10)" ], "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "NaPi", "BUFFER_CONC": "0.02", "MEASURE_KIN": "continuous-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.4, "ln(ku)_H2O": 6.7, "dGKIN_H2O": 4.24, "AUTHOR_KIN": "Ferguson, N., Johnson, C.M., Macias, M., Oschkinat, H., Fersht, A.", "REFERENCE_KIN": "Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. Proc. Natl. Acad. Sci. U.S.A. 98, 13002\u201313007. https://doi.org/10.1073/pnas.221467198", "YEAR_KIN": 2001.0, "PMID_KIN": "11687613", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "SH3 domain of the phosphatidylinositol 3-kinase regulatory subunit alpha", "SOURCE": "Bos taurus", "LENGTH": 84.0, "UniProt": "P23727", "PDB_wild": "1pnj", "MUTATED_CHAIN": "A", "CATH": [ "1pnjA00 (2.30.30.40)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.2, "BUFFER_NAME": "NaPi", "BUFFER_CONC": "0.02", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": -1.04, "ln(ku)_H2O": -7.31, "dGKIN_H2O": 15.27, "AUTHOR_KIN": "Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM", "REFERENCE_KIN": "Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J Mol Biol. 276(3):657-67. https://doi.org/10.1006/jmbi.1997.1553", "YEAR_KIN": 1998.0, "PMID_KIN": "9551103", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "SH3 domain of the phosphatidylinositol 3-kinase regulatory subunit alpha", "SOURCE": "Bos taurus", "LENGTH": 84.0, "UniProt": "P23727", "PDB_wild": "1pnj", "MUTATED_CHAIN": "A", "CATH": [ "1pnjA00 (2.30.30.40)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.2, "BUFFER_NAME": "NaPi", "BUFFER_CONC": "0.02", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": -1.04, "ln(ku)_H2O": -7.31, "dGKIN_H2O": 15.27, "AUTHOR_KIN": "Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM", "REFERENCE_KIN": "Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J Mol Biol. 276(3):657-67. https://doi.org/10.1006/jmbi.1997.1553", "YEAR_KIN": 1998.0, "PMID_KIN": "9551103", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "18th module of muscle protein twitchin", "SOURCE": "Caenorhabditis elegans", "LENGTH": 93.0, "UniProt": "Q23551", "PDB_wild": "1wit", "MUTATED_CHAIN": "A", "PFAM": [ "PF07679" ], "CATH": [ "1witA00 (2.60.40.10)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_PDB": "WT", "T": 20.0, "pH": 5.0, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 0.41, "ln(ku)_H2O": -8.18, "dGKIN_H2O": 20.93, "beta-T": 0.7, "AUTHOR_KIN": "Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39", "REFERENCE_KIN": "Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39. https://doi.org/10.1006/jmbi.1996.0665", "YEAR_KIN": 1996.0, "PMID_KIN": "8969309", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "18th module of muscle protein twitchin", "SOURCE": "Caenorhabditis elegans", "LENGTH": 93.0, "UniProt": "Q23551", "PDB_wild": "1wit", "MUTATED_CHAIN": "A", "PFAM": [ "PF07679" ], "CATH": [ "1witA00 (2.60.40.10)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_PDB": "WT", "T": 20.0, "pH": 5.0, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 0.41, "ln(ku)_H2O": -8.18, "dGKIN_H2O": 20.93, "beta-T": 0.7, "AUTHOR_KIN": "Fong S, Hamill SJ, Proctor M, Freund SM, Benian GM, Chothia C, Bycroft M, Clarke J Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39", "REFERENCE_KIN": "Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J Mol Biol. 264(3):624-39. https://doi.org/10.1006/jmbi.1996.0665", "YEAR_KIN": 1996.0, "PMID_KIN": "8969309", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Acylphosphatase-1", "SOURCE": "Homo sapiens", "LENGTH": 99.0, "UniProt": "P07311", "PDB_wild": "2vh7", "MUTATED_CHAIN": "A", "PFAM": [ "PF00708" ], "CATH": [ "2vh7A00 (3.30.70.100)" ], "EC_NUMBER": "3.6.1.7", "MUTATION_PDB": "WT", "T": 28.0, "pH": 5.5, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 0.84, "ln(ku)_H2O": -6.5, "dGKIN_H2O": 18.37, "mf": -5.1, "mu": 2.0, "CM_KIN": 2.6, "AUTHOR_KIN": "Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G", "REFERENCE_KIN": "Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38(7):2135-42. https://doi.org/10.1021/bi9822630", "YEAR_KIN": 1999.0, "PMID_KIN": "10026297", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Acylphosphatase-1", "SOURCE": "Homo sapiens", "LENGTH": 99.0, "UniProt": "P07311", "PDB_wild": "2vh7", "MUTATED_CHAIN": "A", "PFAM": [ "PF00708" ], "CATH": [ "2vh7A00 (3.30.70.100)" ], "EC_NUMBER": "3.6.1.7", "MUTATION_PDB": "WT", "T": 28.0, "pH": 5.5, "BUFFER_NAME": "Na Acetate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 0.84, "ln(ku)_H2O": -6.5, "dGKIN_H2O": 18.37, "mf": -5.1, "mu": 2.0, "CM_KIN": 2.6, "AUTHOR_KIN": "Taddei N, Chiti F, Paoli P, Fiaschi T, Bucciantini M, Stefani M, Dobson CM, Ramponi G", "REFERENCE_KIN": "Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry 38(7):2135-42. https://doi.org/10.1021/bi9822630", "YEAR_KIN": 1999.0, "PMID_KIN": "10026297", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "apocytochrome b5", "SOURCE": "Bos taurus", "LENGTH": 93.0, "UniProt": "P00171", "PDB_wild": "1cyo", "MUTATED_CHAIN": "A", "PFAM": [ "PF00173" ], "CATH": [ "1cyoA00 (3.10.120.10)" ], "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 2.97, "ln(ku)_H2O": -1.43, "dGKIN_H2O": 10.35, "mf": -5.59, "mu": 2.4, "CM_KIN": 1.58, "AUTHOR_KIN": "Manyusa S, Whitford D", "REFERENCE_KIN": "Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements. Biochemistry 38(29):9533-40. https://doi.org/10.1021/bi990550d", "YEAR_KIN": 1999.0, "PMID_KIN": "10413531", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "apocytochrome b5", "SOURCE": "Bos taurus", "LENGTH": 93.0, "UniProt": "P00171", "PDB_wild": "1cyo", "MUTATED_CHAIN": "A", "PFAM": [ "PF00173" ], "CATH": [ "1cyoA00 (3.10.120.10)" ], "MUTATION_PDB": "WT", "T": 10.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": 2.97, "ln(ku)_H2O": -1.43, "dGKIN_H2O": 10.35, "mf": -5.59, "mu": 2.4, "CM_KIN": 1.58, "AUTHOR_KIN": "Manyusa S, Whitford D", "REFERENCE_KIN": "Defining folding and unfolding reactions of apocytochrome b5 using equilibrium and kinetic fluorescence measurements. Biochemistry 38(29):9533-40. https://doi.org/10.1021/bi990550d", "YEAR_KIN": 1999.0, "PMID_KIN": "10413531", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "hbLBD (Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial)", "SOURCE": "Homo sapiens", "LENGTH": 84.0, "UniProt": "P11182", "PDB_wild": "1k8m", "MUTATED_CHAIN": "A", "PFAM": [ "PF00364" ], "CATH": [ "1k8mA00 (2.40.50.100)" ], "EC_NUMBER": "2.3.1.168", "MUTATION_PDB": "WT", "T": 22.0, "pH": 7.5, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "urea", "ln(kf)_H2O": -0.94, "ln(ku)_H2O": -8.05, "dGKIN_H2O": 17.45, "mf": -1.2, "mu": 0.98, "CM_KIN": 4.8, "AUTHOR_KIN": "Naik MT, Chang YC, Huang TH", "REFERENCE_KIN": "Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex. FEBS Lett. 530(1-3):133-8. https://doi.org/10.1016/s0014-5793(02)03444-0", "YEAR_KIN": 2002.0, "PMID_KIN": "12387880", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "hbLBD (Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial)", "SOURCE": "Homo sapiens", "LENGTH": 84.0, "UniProt": "P11182", "PDB_wild": "1k8m", "MUTATED_CHAIN": "A", "PFAM": [ "PF00364" ], "CATH": [ "1k8mA00 (2.40.50.100)" ], "EC_NUMBER": "2.3.1.168", "MUTATION_PDB": "WT", "T": 22.0, "pH": 7.5, "BUFFER_NAME": "KPi", "BUFFER_CONC": "0.05", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "urea", "ln(kf)_H2O": -0.94, "ln(ku)_H2O": -8.05, "dGKIN_H2O": 17.45, "mf": -1.2, "mu": 0.98, "CM_KIN": 4.8, "AUTHOR_KIN": "Naik MT, Chang YC, Huang TH", "REFERENCE_KIN": "Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex. FEBS Lett. 530(1-3):133-8. https://doi.org/10.1016/s0014-5793(02)03444-0", "YEAR_KIN": 2002.0, "PMID_KIN": "12387880", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Protein p13 MTCP-1", "SOURCE": "Homo sapiens", "LENGTH": 117.0, "UniProt": "P56278", "PDB_wild": "1qtu", "MUTATED_CHAIN": "A", "PFAM": [ "PF01840" ], "CATH": [ "1qtuA00 (2.40.15.10)" ], "MUTATION_PDB": "WT", "T": 21.0, "pH": 7.0, "BUFFER_NAME": "Tris", "BUFFER_CONC": "0.05", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": -0.36, "ln(ku)_H2O": -11.11, "dGKIN_H2O": 26.28, "mf": -9.76, "mu": 3.0, "CM_KIN": 2.2, "AUTHOR_KIN": "Roumestand C, Boyer M, Guignard L, Barthe P, Royer CA", "REFERENCE_KIN": "Characterization of the folding and unfolding reactions of a small beta-barrel protein of novel topology, the MTCP1 oncogene product P13. J Mol Biol. 312(1):247-59. https://doi.org/10.1006/jmbi.2001.4928", "YEAR_KIN": 2001.0, "PMID_KIN": "11545600", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Protein p13 MTCP-1", "SOURCE": "Homo sapiens", "LENGTH": 117.0, "UniProt": "P56278", "PDB_wild": "1qtu", "MUTATED_CHAIN": "A", "PFAM": [ "PF01840" ], "CATH": [ "1qtuA00 (2.40.15.10)" ], "MUTATION_PDB": "WT", "T": 21.0, "pH": 7.0, "BUFFER_NAME": "Tris", "BUFFER_CONC": "0.05", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "GdmCl", "ln(kf)_H2O": -0.36, "ln(ku)_H2O": -11.11, "dGKIN_H2O": 26.28, "mf": -9.76, "mu": 3.0, "CM_KIN": 2.2, "AUTHOR_KIN": "Roumestand C, Boyer M, Guignard L, Barthe P, Royer CA", "REFERENCE_KIN": "Characterization of the folding and unfolding reactions of a small beta-barrel protein of novel topology, the MTCP1 oncogene product P13. J Mol Biol. 312(1):247-59. https://doi.org/10.1006/jmbi.2001.4928", "YEAR_KIN": 2001.0, "PMID_KIN": "11545600", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Trp-cage protein", "LENGTH": 20.0, "PDB_wild": "1l2y", "MUTATED_CHAIN": "A", "MUTATION_PDB": "WT", "T": 23.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.1", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 12.39, "ln(ku)_H2O": 11.32, "dGKIN_H2O": 2.62, "AUTHOR_KIN": "Qiu L, Pabit SA, Roitberg AE, Hagen SJ", "REFERENCE_KIN": "Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros. J Am Chem Soc. 124(44):12952-3. https://doi.org/10.1021/ja0279141", "YEAR_KIN": 2002.0, "PMID_KIN": "12405814", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Trp-cage protein", "LENGTH": 20.0, "PDB_wild": "1l2y", "MUTATED_CHAIN": "A", "MUTATION_PDB": "WT", "T": 23.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.1", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation", "ln(kf)_H2O": 12.39, "ln(ku)_H2O": 11.32, "dGKIN_H2O": 2.62, "AUTHOR_KIN": "Qiu L, Pabit SA, Roitberg AE, Hagen SJ", "REFERENCE_KIN": "Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros. J Am Chem Soc. 124(44):12952-3. https://doi.org/10.1021/ja0279141", "YEAR_KIN": 2002.0, "PMID_KIN": "12405814", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "\u03b13D", "LENGTH": 73.0, "PDB_wild": "2a3d", "MUTATED_CHAIN": "A", "MUTATION_PDB": "WT", "T": 25.0, "pH": 2.2, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation or urea", "ln(kf)_H2O": 12.24, "ln(ku)_H2O": 7.83, "dGKIN_H2O": 10.93, "AUTHOR_KIN": "Zhu Y, Alonso DO, Maki K, Huang CY, Lahr SJ, Daggett V, Roder H, DeGrado WF, Gai F", "REFERENCE_KIN": "Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein. Proc Natl Acad Sci U S A. 100(26):15486-91. https://doi.org/10.1073/pnas.2136623100", "YEAR_KIN": 2003.0, "PMID_KIN": "14671331", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "\u03b13D", "LENGTH": 73.0, "PDB_wild": "2a3d", "MUTATED_CHAIN": "A", "MUTATION_PDB": "WT", "T": 25.0, "pH": 2.2, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "T-jump", "METHOD_KIN": "thermal denaturation or urea", "ln(kf)_H2O": 12.24, "ln(ku)_H2O": 7.83, "dGKIN_H2O": 10.93, "AUTHOR_KIN": "Zhu Y, Alonso DO, Maki K, Huang CY, Lahr SJ, Daggett V, Roder H, DeGrado WF, Gai F", "REFERENCE_KIN": "Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein. Proc Natl Acad Sci U S A. 100(26):15486-91. https://doi.org/10.1073/pnas.2136623100", "YEAR_KIN": 2003.0, "PMID_KIN": "14671331", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Villin-1", "SOURCE": "Gallus gallus", "LENGTH": 126.0, "UniProt": "P02640", "PDB_wild": "2vik", "MUTATED_CHAIN": "A", "PFAM": [ "PF00626" ], "CATH": [ "2vikA00 (3.40.20.10)" ], "MUTATION_PDB": "WT", "T": 37.0, "pH": 4.1, "BUFFER_NAME": "Acetate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM beta-ME", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.8, "ln(ku)_H2O": -2.8, "dGKIN_H2O": 24.74, "mf": -4.64, "mu": 1.72, "AUTHOR_KIN": "Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI", "REFERENCE_KIN": "Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry. 37(41):14508-18. https://doi.org/10.1021/bi980889k", "YEAR_KIN": 1998.0, "PMID_KIN": "9772179", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Villin-1", "SOURCE": "Gallus gallus", "LENGTH": 126.0, "UniProt": "P02640", "PDB_wild": "2vik", "MUTATED_CHAIN": "A", "PFAM": [ "PF00626" ], "CATH": [ "2vikA00 (3.40.20.10)" ], "MUTATION_PDB": "WT", "T": 37.0, "pH": 4.1, "BUFFER_NAME": "Acetate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM beta-ME", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.8, "ln(ku)_H2O": -2.8, "dGKIN_H2O": 24.74, "mf": -4.64, "mu": 1.72, "AUTHOR_KIN": "Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI", "REFERENCE_KIN": "Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry. 37(41):14508-18. https://doi.org/10.1021/bi980889k", "YEAR_KIN": 1998.0, "PMID_KIN": "9772179", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "C-domain of development-specific protein S", "SOURCE": "Myxococcus xanthus", "LENGTH": 90.0, "UniProt": "P02966", "PDB_wild": "1prs", "MUTATED_CHAIN": "A", "PFAM": [ "PF00030" ], "CATH": [ "1prsA01 (2.60.20.10)", "1prsA02 (2.60.20.10)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.025", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "urea", "ln(kf)_H2O": -2.04, "ln(ku)_H2O": -9.25, "dGKIN_H2O": 17.56, "AUTHOR_KIN": "Wenk M, Jaenicke R, Mayr EM", "REFERENCE_KIN": "Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438(1-2):127-30.https://doi.org/10.1016/s0014-5793(98)01287-3", "YEAR_KIN": 1998.0, "PMID_KIN": "9821973", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "C-domain of development-specific protein S", "SOURCE": "Myxococcus xanthus", "LENGTH": 90.0, "UniProt": "P02966", "PDB_wild": "1prs", "MUTATED_CHAIN": "A", "PFAM": [ "PF00030" ], "CATH": [ "1prsA01 (2.60.20.10)", "1prsA02 (2.60.20.10)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.025", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "urea", "ln(kf)_H2O": -2.04, "ln(ku)_H2O": -9.25, "dGKIN_H2O": 17.56, "AUTHOR_KIN": "Wenk M, Jaenicke R, Mayr EM", "REFERENCE_KIN": "Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438(1-2):127-30.https://doi.org/10.1016/s0014-5793(98)01287-3", "YEAR_KIN": 1998.0, "PMID_KIN": "9821973", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "N-domain of development-specific protein S", "SOURCE": "Myxococcus xanthus", "LENGTH": 82.0, "UniProt": "P02966", "PDB_wild": "1prs", "MUTATED_CHAIN": "A", "PFAM": [ "PF00030" ], "CATH": [ "1prsA01 (2.60.20.10)", "1prsA02 (2.60.20.10)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.025", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "urea", "ln(kf)_H2O": 3.04, "ln(ku)_H2O": -9.37, "dGKIN_H2O": 30.23, "AUTHOR_KIN": "Wenk M, Jaenicke R, Mayr EM", "REFERENCE_KIN": "Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438(1-2):127-30. https://doi.org/10.1016/s0014-5793(98)01287-3", "YEAR_KIN": 1998.0, "PMID_KIN": "9821973", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "N-domain of development-specific protein S", "SOURCE": "Myxococcus xanthus", "LENGTH": 82.0, "UniProt": "P02966", "PDB_wild": "1prs", "MUTATED_CHAIN": "A", "PFAM": [ "PF00030" ], "CATH": [ "1prsA01 (2.60.20.10)", "1prsA02 (2.60.20.10)" ], "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.0, "BUFFER_NAME": "MOPS", "BUFFER_CONC": "0.025", "MEASURE_KIN": "manual mixing", "METHOD_KIN": "urea", "ln(kf)_H2O": 3.04, "ln(ku)_H2O": -9.37, "dGKIN_H2O": 30.23, "AUTHOR_KIN": "Wenk M, Jaenicke R, Mayr EM", "REFERENCE_KIN": "Kinetic stabilisation of a modular protein by domain interactions. FEBS Lett. 438(1-2):127-30. https://doi.org/10.1016/s0014-5793(98)01287-3", "YEAR_KIN": 1998.0, "PMID_KIN": "9821973", "STATE": "Yes", "REVIEW_DATE": "2023-06-09T01:00:00" }, { "PROTEIN": "Azurin", "SOURCE": "Pseudomonas aeruginosa", "LENGTH": 128.0, "UniProt": "P00282", "PDB_wild": "1azu", "MUTATED_CHAIN": "A", "PFAM": [ "PF00127" ], "CATH": [ "1azuA00 (2.60.40.420)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "TRIS", "BUFFER_CONC": "0.1", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GuHCl", "ln(kf)_H2O": 4.84, "ln(ku)_H2O": -16.96, "AUTHOR_KIN": "Wilson, C.J., Wittung-Stafshede, P.", "REFERENCE_KIN": "Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054\u201310062. https://doi.org/10.1021/bi050342n", "YEAR_KIN": 2005.0, "PMID_KIN": "16042382", "STATE": "2", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "Azurin", "SOURCE": "Pseudomonas aeruginosa", "LENGTH": 128.0, "UniProt": "P00282", "PDB_wild": "1azu", "MUTATED_CHAIN": "A", "PFAM": [ "PF00127" ], "CATH": [ "1azuA00 (2.60.40.420)" ], "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "TRIS", "BUFFER_CONC": "0.1", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "GuHCl", "ln(kf)_H2O": 4.84, "ln(ku)_H2O": -16.96, "AUTHOR_KIN": "Wilson, C.J., Wittung-Stafshede, P.", "REFERENCE_KIN": "Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry 44, 10054\u201310062. https://doi.org/10.1021/bi050342n", "YEAR_KIN": 2005.0, "PMID_KIN": "16042382", "STATE": "2", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "CBP, KIX domain", "SOURCE": "Mus musculus", "LENGTH": 86.0, "UniProt": "P45481", "PDB_wild": "1sb0", "MUTATED_CHAIN": "A", "PFAM": [ "PF02172" ], "CATH": [ "1sb0A00 (1.10.246.20)" ], "EC_NUMBER": "2.3.1.48", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.78, "ln(ku)_H2O": 2.65, "dGKIN_H2O": 12.5, "mf": -3.18, "mu": 0.84, "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S", "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289", "YEAR_KIN": 2017.0, "PMID_KIN": "28459531", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" }, { "PROTEIN": "CBP, KIX domain", "SOURCE": "Mus musculus", "LENGTH": 86.0, "UniProt": "P45481", "PDB_wild": "1sb0", "MUTATED_CHAIN": "A", "PFAM": [ "PF02172" ], "CATH": [ "1sb0A00 (1.10.246.20)" ], "EC_NUMBER": "2.3.1.48", "MUTATION_UNIPROT": "WT", "MUTATION_PDB": "WT", "T": 20.0, "pH": 7.2, "BUFFER_NAME": "Sodium Phosphate", "BUFFER_CONC": "0.05", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.78, "ln(ku)_H2O": 2.65, "dGKIN_H2O": 12.5, "mf": -3.18, "mu": 0.84, "AUTHOR_KIN": "Troilo F, Bonetti D, Toto A, Visconti L, Brunori M, Longhi S, Gianni S", "REFERENCE_KIN": "The Folding Pathway of the KIX Domain. ACS Chem Biol. 12(6):1683-1690. https://doi.org/10.1021/acschembio.7b00289", "YEAR_KIN": 2017.0, "PMID_KIN": "28459531", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-11T01:00:00" } ]