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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.089", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "T68A", "MUTATION_PDB": "T68A", "SEC_STR": "Coil", "RSA": "31.7", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.26, "dln(kf)_H2O": 0.54, "ln(ku)_H2O": -3.0, "dGKIN_H2O": 27.88, "ddGKIN_H2O": 1.32, "mf": -3.15, "mu": 1.16, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.090", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "T68A", "MUTATION_PDB": "T68A", "SEC_STR": "Coil", "RSA": "31.7", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.26, "dln(kf)_H2O": 0.54, "ln(ku)_H2O": -3.0, "dGKIN_H2O": 27.88, "ddGKIN_H2O": 1.32, "mf": -3.15, "mu": 1.16, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.090", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "V69A", "MUTATION_PDB": "V69A", "SEC_STR": "Beta", "RSA": "59.9", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.52, "dln(kf)_H2O": -1.2, "ln(ku)_H2O": -2.41, "dln(ku)_H2O": 0.59, "dGKIN_H2O": 22.12, "ddGKIN_H2O": -4.44, "mf": -3.05, "mu": 1.02, "PhiF_H2O": 0.72, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.100", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "C81I", "MUTATION_PDB": "C81I", "SEC_STR": "Helix", "RSA": "2.2", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 10.12, "dln(kf)_H2O": 2.4, "ln(ku)_H2O": -0.78, "dln(ku)_H2O": 2.22, "dGKIN_H2O": 27.0, "ddGKIN_H2O": 0.44, "mf": -3.77, "mu": 0.94, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.101", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "L82A", "MUTATION_PDB": "L82A", "SEC_STR": "Helix", "RSA": "3.7", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.12, "dln(kf)_H2O": -1.6, "ln(ku)_H2O": -0.16, "dln(ku)_H2O": 2.84, "dGKIN_H2O": 15.56, "ddGKIN_H2O": -11.0, "mf": -4.61, "mu": 1.14, "PhiF_H2O": 0.39, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.105", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "R89L", "MUTATION_PDB": "R89L", "SEC_STR": "Helix", "RSA": "33.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 10.33, "dln(kf)_H2O": 2.61, "ln(ku)_H2O": -3.22, "dln(ku)_H2O": -0.22, "dGKIN_H2O": 33.57, "ddGKIN_H2O": 7.01, "mf": -3.12, "mu": 1.14, "PhiF_H2O": 1.2, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.109", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "C96L", "MUTATION_PDB": "C96L", "SEC_STR": "Beta", "RSA": "14.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.36, "dln(kf)_H2O": -0.36, "ln(ku)_H2O": -3.22, "dln(ku)_H2O": -0.22, "dGKIN_H2O": 26.22, "ddGKIN_H2O": -0.34, "mf": -2.73, "mu": 1.21, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.110", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "C96L", "MUTATION_PDB": "C96L", "SEC_STR": "Beta", "RSA": "14.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.36, "dln(kf)_H2O": -0.36, "ln(ku)_H2O": -3.22, "dln(ku)_H2O": -0.22, "dGKIN_H2O": 26.22, "ddGKIN_H2O": -0.34, "mf": -2.73, "mu": 1.21, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.110", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "C96M", "MUTATION_PDB": "C96M", "SEC_STR": "Beta", "RSA": "14.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.9, "dln(kf)_H2O": 0.18, "ln(ku)_H2O": -3.51, "dln(ku)_H2O": -0.51, "dGKIN_H2O": 28.26, "ddGKIN_H2O": 1.7, "mf": -3.1, "mu": 1.16, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.111", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "C96M", "MUTATION_PDB": "C96M", "SEC_STR": "Beta", "RSA": "14.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.9, "dln(kf)_H2O": 0.18, "ln(ku)_H2O": -3.51, "dln(ku)_H2O": -0.51, "dGKIN_H2O": 28.26, "ddGKIN_H2O": 1.7, "mf": -3.1, "mu": 1.16, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.111", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "A97G", "MUTATION_PDB": "A97G", "SEC_STR": "Beta", "RSA": "0.9", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.05, "dln(kf)_H2O": -0.67, "ln(ku)_H2O": -1.56, "dln(ku)_H2O": 1.44, "dGKIN_H2O": 21.33, "ddGKIN_H2O": -5.23, "mf": -2.9, "mu": 0.92, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.112", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "A97G", "MUTATION_PDB": "A97G", "SEC_STR": "Beta", "RSA": "0.9", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.05, "dln(kf)_H2O": -0.67, "ln(ku)_H2O": -1.56, "dln(ku)_H2O": 1.44, "dGKIN_H2O": 21.33, "ddGKIN_H2O": -5.23, "mf": -2.9, "mu": 0.92, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.112", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "V98A", "MUTATION_PDB": "V98A", "SEC_STR": "Beta", "RSA": "2.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.73, "dln(kf)_H2O": -1.99, "ln(ku)_H2O": -1.24, "dln(ku)_H2O": 1.76, "dGKIN_H2O": 17.26, "ddGKIN_H2O": -9.3, "mf": -2.28, "mu": 0.92, "PhiF_H2O": 0.48, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.113", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "V98A", "MUTATION_PDB": "V98A", "SEC_STR": "Beta", "RSA": "2.1", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.73, "dln(kf)_H2O": -1.99, "ln(ku)_H2O": -1.24, "dln(ku)_H2O": 1.76, "dGKIN_H2O": 17.26, "ddGKIN_H2O": -9.3, "mf": -2.28, "mu": 0.92, "PhiF_H2O": 0.48, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.114", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "E104A", "MUTATION_PDB": "E104A", "SEC_STR": "Coil", "RSA": "61.3", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.08, "dln(kf)_H2O": 0.36, "ln(ku)_H2O": -2.53, "dln(ku)_H2O": 0.47, "dGKIN_H2O": 26.28, "ddGKIN_H2O": -0.28, "mf": -3.2, "mu": 0.92, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.115", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "E104A", "MUTATION_PDB": "E104A", "SEC_STR": "Coil", "RSA": "61.3", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.08, "dln(kf)_H2O": 0.36, "ln(ku)_H2O": -2.53, "dln(ku)_H2O": 0.47, "dGKIN_H2O": 26.28, "ddGKIN_H2O": -0.28, "mf": -3.2, "mu": 0.92, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.115", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "K109A", "MUTATION_PDB": "K109A", "SEC_STR": "Coil", "RSA": "22.0", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.01, "dln(kf)_H2O": 0.29, "ln(ku)_H2O": -1.66, "dln(ku)_H2O": 1.34, "dGKIN_H2O": 23.97, "ddGKIN_H2O": -2.59, "mf": -3.25, "mu": 0.84, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.116", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "K109A", "MUTATION_PDB": "K109A", "SEC_STR": "Coil", "RSA": "22.0", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 8.01, "dln(kf)_H2O": 0.29, "ln(ku)_H2O": -1.66, "dln(ku)_H2O": 1.34, "dGKIN_H2O": 23.97, "ddGKIN_H2O": -2.59, "mf": -3.25, "mu": 0.84, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.116", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "L112A", "MUTATION_PDB": "L112A", "SEC_STR": "Coil", "RSA": "15.2", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.07, "dln(kf)_H2O": -1.65, "ln(ku)_H2O": 1.01, "dln(ku)_H2O": 4.01, "dGKIN_H2O": 12.54, "ddGKIN_H2O": -14.02, "mf": -2.48, "mu": 0.89, "PhiF_H2O": 0.41, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.119", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "A118L", "MUTATION_PDB": "A118L", "SEC_STR": "Helix", "RSA": "1.9", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.28, "dln(kf)_H2O": -0.44, "ln(ku)_H2O": 1.17, "dln(ku)_H2O": 4.17, "dGKIN_H2O": 15.14, "ddGKIN_H2O": -11.42, "mf": -2.85, "mu": 0.77, "PhiF_H2O": 0.11, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.120", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "A118L", "MUTATION_PDB": "A118L", "SEC_STR": "Helix", "RSA": "1.9", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.28, "dln(kf)_H2O": -0.44, "ln(ku)_H2O": 1.17, "dln(ku)_H2O": 4.17, "dGKIN_H2O": 15.14, "ddGKIN_H2O": -11.42, "mf": -2.85, "mu": 0.77, "PhiF_H2O": 0.11, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. 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J. Mol. 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J. Mol. 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J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.122", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "E124A", "MUTATION_PDB": "E124A", "SEC_STR": "Coil", "RSA": "22.2", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.55, "dln(kf)_H2O": -0.17, "ln(ku)_H2O": -2.66, "dln(ku)_H2O": 0.34, "dGKIN_H2O": 25.31, "ddGKIN_H2O": -1.25, "mf": -3.0, "mu": 0.99, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.122", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "E125A", "MUTATION_PDB": "E125A", "SEC_STR": "Beta", "RSA": "24.7", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.81, "ln(ku)_H2O": -2.81, "dln(ku)_H2O": 0.19, "dGKIN_H2O": 24.09, "ddGKIN_H2O": -2.47, "mf": -3.0, "mu": 1.07, "PhiF_H2O": 0.86, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.123", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "E125A", "MUTATION_PDB": "E125A", "SEC_STR": "Beta", "RSA": "24.7", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 6.91, "dln(kf)_H2O": -0.81, "ln(ku)_H2O": -2.81, "dln(ku)_H2O": 0.19, "dGKIN_H2O": 24.09, "ddGKIN_H2O": -2.47, "mf": -3.0, "mu": 1.07, "PhiF_H2O": 0.86, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.123", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "L126A", "MUTATION_PDB": "L126A", "SEC_STR": "Beta", "RSA": "2.4", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.34, "dln(kf)_H2O": -2.38, "ln(ku)_H2O": 0.83, "dln(ku)_H2O": 3.83, "dGKIN_H2O": 11.16, "ddGKIN_H2O": -15.4, "mf": -3.32, "mu": 0.79, "PhiF_H2O": 0.45, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.124", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "L126A", "MUTATION_PDB": "L126A", "SEC_STR": "Beta", "RSA": "2.4", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.34, "dln(kf)_H2O": -2.38, "ln(ku)_H2O": 0.83, "dln(ku)_H2O": 3.83, "dGKIN_H2O": 11.16, "ddGKIN_H2O": -15.4, "mf": -3.32, "mu": 0.79, "PhiF_H2O": 0.45, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.124", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "V128A", "MUTATION_PDB": "V128A", "SEC_STR": "Beta", "RSA": "0.0", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.5, "dln(kf)_H2O": -2.22, "ln(ku)_H2O": 1.16, "dln(ku)_H2O": 4.16, "dGKIN_H2O": 10.74, "ddGKIN_H2O": -15.82, "mf": -3.0, "mu": 0.82, "PhiF_H2O": 0.42, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.125", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "V128A", "MUTATION_PDB": "V128A", "SEC_STR": "Beta", "RSA": "0.0", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 5.5, "dln(kf)_H2O": -2.22, "ln(ku)_H2O": 1.16, "dln(ku)_H2O": 4.16, "dGKIN_H2O": 10.74, "ddGKIN_H2O": -15.82, "mf": -3.0, "mu": 0.82, "PhiF_H2O": 0.42, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.125", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "D129A", "MUTATION_PDB": "D129A", "SEC_STR": "Beta", "RSA": "20.2", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.43, "dln(kf)_H2O": -0.29, "ln(ku)_H2O": -2.41, "dln(ku)_H2O": 0.59, "dGKIN_H2O": 24.37, "ddGKIN_H2O": -2.19, "mf": -3.1, "mu": 1.14, "PhiF_H2O": 0.38, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.126", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" }, { "PROTEIN": "raf RBD", "SOURCE": "Homo sapiens", "LENGTH": 79.0, "UniProt": "P04049", "PDB_wild": "1rfa", "MUTATED_CHAIN": "A", "PFAM": [ "PF02196" ], "CATH": [ "1rfaA00 (3.10.20.90)" ], "EC_NUMBER": "2.7.11.1", "MUTATION_UNIPROT": "D129A", "MUTATION_PDB": "D129A", "SEC_STR": "Beta", "RSA": "20.2", "T": 25.0, "pH": 7.0, "BUFFER_NAME": "Phosphate", "BUFFER_CONC": "0.05", "ADDITIVES": "1 mM DTT", "MEASURE_KIN": "stopped-flow", "METHOD_KIN": "urea", "ln(kf)_H2O": 7.43, "dln(kf)_H2O": -0.29, "ln(ku)_H2O": -2.41, "dln(ku)_H2O": 0.59, "dGKIN_H2O": 24.37, "ddGKIN_H2O": -2.19, "mf": -3.1, "mu": 1.14, "PhiF_H2O": 0.38, "AUTHOR_KIN": "Campbell-Valois, F.-X., Michnick, S.W.", "REFERENCE_KIN": "The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse. J. Mol. Biol. 365, 1559\u20131577. https://doi.org/10.1016/j.jmb.2006.10.126", "YEAR_KIN": 2007.0, "PMID_KIN": "17137592", "STATE": "2", "REVERSIBILITY": "yes", "REVIEW_DATE": "2023-06-04T01:00:00" } ]