[
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127G",
      "MUTATION_PDB": "D127G",
      "SEC_STR": "Helix",
      "RSA": "62.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127G",
      "MUTATION_PDB": "D127G",
      "SEC_STR": "Helix",
      "RSA": "62.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128A",
      "MUTATION_PDB": "S128A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128A",
      "MUTATION_PDB": "S128A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128G",
      "MUTATION_PDB": "S128G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S128G",
      "MUTATION_PDB": "S128G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I129A",
      "MUTATION_PDB": "I129A",
      "SEC_STR": "Helix",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I129A",
      "MUTATION_PDB": "I129A",
      "SEC_STR": "Helix",
      "RSA": "2.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131A",
      "MUTATION_PDB": "D131A",
      "SEC_STR": "Helix",
      "RSA": "78.5",
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131A",
      "MUTATION_PDB": "D131A",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131G",
      "MUTATION_PDB": "D131G",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D131G",
      "MUTATION_PDB": "D131G",
      "SEC_STR": "Helix",
      "RSA": "78.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132A",
      "MUTATION_PDB": "R132A",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132A",
      "MUTATION_PDB": "R132A",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132G",
      "MUTATION_PDB": "R132G",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R132G",
      "MUTATION_PDB": "R132G",
      "SEC_STR": "Helix",
      "RSA": "65.7",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Y133A",
      "MUTATION_PDB": "Y133A",
      "SEC_STR": "Coil",
      "RSA": "31.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Y133A",
      "MUTATION_PDB": "Y133A",
      "SEC_STR": "Coil",
      "RSA": "31.5",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138A",
      "MUTATION_PDB": "T138A",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138A",
      "MUTATION_PDB": "T138A",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "T138G",
      "MUTATION_PDB": "T138G",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
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      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D139A",
      "MUTATION_PDB": "D139A",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D139A",
      "MUTATION_PDB": "D139A",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
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      "MUTATION_UNIPROT": "D139G",
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
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         "1e41A00 (1.10.533.10)"
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1e41A00 (1.10.533.10)"
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      "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,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1e41A00 (1.10.533.10)"
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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         "1e41A00 (1.10.533.10)"
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      "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,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "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,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "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,
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "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",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
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      "SOURCE": "Homo sapiens",
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      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
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      "SOURCE": "Homo sapiens",
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         "1e41A00 (1.10.533.10)"
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      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D143A",
      "MUTATION_PDB": "D143A",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D143G",
      "MUTATION_PDB": "D143G",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D143G",
      "MUTATION_PDB": "D143G",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S144A",
      "MUTATION_PDB": "S144A",
      "SEC_STR": "Helix",
      "RSA": "2.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 8.79,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S144A",
      "MUTATION_PDB": "S144A",
      "SEC_STR": "Helix",
      "RSA": "2.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 8.79,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L145M",
      "MUTATION_PDB": "L145M",
      "SEC_STR": "Helix",
      "RSA": "12.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L145M",
      "MUTATION_PDB": "L145M",
      "SEC_STR": "Helix",
      "RSA": "12.8",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146A",
      "MUTATION_PDB": "R146A",
      "SEC_STR": "Helix",
      "RSA": "60.9",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146A",
      "MUTATION_PDB": "R146A",
      "SEC_STR": "Helix",
      "RSA": "60.9",
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      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146G",
      "MUTATION_PDB": "R146G",
      "SEC_STR": "Helix",
      "RSA": "60.9",
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      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R146G",
      "MUTATION_PDB": "R146G",
      "SEC_STR": "Helix",
      "RSA": "60.9",
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      "BUFFER_NAME": "Phosphate",
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      "METHOD_KIN": "Urea",
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W148F",
      "MUTATION_PDB": "W148F",
      "SEC_STR": "Helix",
      "RSA": "4.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W148F",
      "MUTATION_PDB": "W148F",
      "SEC_STR": "Helix",
      "RSA": "4.4",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150A",
      "MUTATION_PDB": "N150A",
      "SEC_STR": "Helix",
      "RSA": "66.2",
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      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150A",
      "MUTATION_PDB": "N150A",
      "SEC_STR": "Helix",
      "RSA": "66.2",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150G",
      "MUTATION_PDB": "N150G",
      "SEC_STR": "Helix",
      "RSA": "66.2",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N150G",
      "MUTATION_PDB": "N150G",
      "SEC_STR": "Helix",
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      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "H160A",
      "MUTATION_PDB": "H160A",
      "SEC_STR": "Helix",
      "RSA": "8.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "H160A",
      "MUTATION_PDB": "H160A",
      "SEC_STR": "Helix",
      "RSA": "8.7",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L161A",
      "MUTATION_PDB": "L161A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L161A",
      "MUTATION_PDB": "L161A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V162A",
      "MUTATION_PDB": "V162A",
      "SEC_STR": "Helix",
      "RSA": "3.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V162A",
      "MUTATION_PDB": "V162A",
      "SEC_STR": "Helix",
      "RSA": "3.5",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L165A",
      "MUTATION_PDB": "L165A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L165A",
      "MUTATION_PDB": "L165A",
      "SEC_STR": "Helix",
      "RSA": "0.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166A",
      "MUTATION_PDB": "R166A",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166A",
      "MUTATION_PDB": "R166A",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166G",
      "MUTATION_PDB": "R166G",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R166G",
      "MUTATION_PDB": "R166G",
      "SEC_STR": "Helix",
      "RSA": "48.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167A",
      "MUTATION_PDB": "S167A",
      "SEC_STR": "Helix",
      "RSA": "59.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167A",
      "MUTATION_PDB": "S167A",
      "SEC_STR": "Helix",
      "RSA": "59.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167G",
      "MUTATION_PDB": "S167G",
      "SEC_STR": "Helix",
      "RSA": "59.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "S167G",
      "MUTATION_PDB": "S167G",
      "SEC_STR": "Helix",
      "RSA": "59.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.11,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C168A",
      "MUTATION_PDB": "C168A",
      "SEC_STR": "Coil",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C168A",
      "MUTATION_PDB": "C168A",
      "SEC_STR": "Coil",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V173A",
      "MUTATION_PDB": "V173A",
      "SEC_STR": "Helix",
      "RSA": "7.0",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V173A",
      "MUTATION_PDB": "V173A",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175A",
      "MUTATION_PDB": "D175A",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175A",
      "MUTATION_PDB": "D175A",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175G",
      "MUTATION_PDB": "D175G",
      "SEC_STR": "Helix",
      "RSA": "46.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D175G",
      "MUTATION_PDB": "D175G",
      "SEC_STR": "Helix",
      "RSA": "46.0",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L176A",
      "MUTATION_PDB": "L176A",
      "SEC_STR": "Helix",
      "RSA": "40.2",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L176A",
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      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
      ],
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V177A",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178A",
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      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178A",
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      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
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      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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         "1e41A00 (1.10.533.10)"
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      "MUTATION_UNIPROT": "Q178G",
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      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
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      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "Q178G",
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      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V180A",
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      "SEC_STR": "Helix",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
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      "MUTATED_CHAIN": "A",
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         "1e41A00 (1.10.533.10)"
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      "MUTATION_UNIPROT": "WT",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "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": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98A",
      "MUTATION_PDB": "C98A",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.53,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98A",
      "MUTATION_PDB": "C98A",
      "SEC_STR": "Helix",
      "RSA": "45.2",
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      "BUFFER_NAME": "Phosphate",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 7.53,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98G",
      "MUTATION_PDB": "C98G",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "C98G",
      "MUTATION_PDB": "C98G",
      "SEC_STR": "Helix",
      "RSA": "45.2",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "F101A",
      "MUTATION_PDB": "F101A",
      "SEC_STR": "Helix",
      "RSA": "26.4",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "F101A",
      "MUTATION_PDB": "F101A",
      "SEC_STR": "Helix",
      "RSA": "26.4",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102A",
      "MUTATION_PDB": "N102A",
      "SEC_STR": "Helix",
      "RSA": "53.5",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
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      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102A",
      "MUTATION_PDB": "N102A",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102G",
      "MUTATION_PDB": "N102G",
      "SEC_STR": "Helix",
      "RSA": "53.5",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "N102G",
      "MUTATION_PDB": "N102G",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.44,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V103A",
      "MUTATION_PDB": "V103A",
      "SEC_STR": "Helix",
      "RSA": "1.4",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "V103A",
      "MUTATION_PDB": "V103A",
      "SEC_STR": "Helix",
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      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I104A",
      "MUTATION_PDB": "I104A",
      "SEC_STR": "Helix",
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I104A",
      "MUTATION_PDB": "I104A",
      "SEC_STR": "Helix",
      "RSA": "3.6",
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      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W112A",
      "MUTATION_PDB": "W112A",
      "SEC_STR": "Helix",
      "RSA": "0.9",
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      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "W112A",
      "MUTATION_PDB": "W112A",
      "SEC_STR": "Helix",
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      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113A",
      "MUTATION_PDB": "R113A",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113A",
      "MUTATION_PDB": "R113A",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113G",
      "MUTATION_PDB": "R113G",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R113G",
      "MUTATION_PDB": "R113G",
      "SEC_STR": "Helix",
      "RSA": "21.0",
      "T": 25.0,
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      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 4.6,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114A",
      "MUTATION_PDB": "R114A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114A",
      "MUTATION_PDB": "R114A",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114G",
      "MUTATION_PDB": "R114G",
      "SEC_STR": "Helix",
      "RSA": "32.3",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.69,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R114G",
      "MUTATION_PDB": "R114G",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L115M",
      "MUTATION_PDB": "L115M",
      "SEC_STR": "Helix",
      "RSA": "1.2",
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      "METHOD_KIN": "Urea",
      "mu": 5.86,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L115M",
      "MUTATION_PDB": "L115M",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117A",
      "MUTATION_PDB": "R117A",
      "SEC_STR": "Helix",
      "RSA": "64.5",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117A",
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      "SEC_STR": "Helix",
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      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117G",
      "MUTATION_PDB": "R117G",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "R117G",
      "MUTATION_PDB": "R117G",
      "SEC_STR": "Helix",
      "RSA": "64.5",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
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      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L119M",
      "MUTATION_PDB": "L119M",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "L119M",
      "MUTATION_PDB": "L119M",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
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         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I126A",
      "MUTATION_PDB": "I126A",
      "SEC_STR": "Helix",
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      "METHOD_KIN": "Urea",
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      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "I126A",
      "MUTATION_PDB": "I126A",
      "SEC_STR": "Helix",
      "RSA": "3.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 5.02,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127A",
      "MUTATION_PDB": "D127A",
      "SEC_STR": "Helix",
      "RSA": "62.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   },
   {
      "PROTEIN": "FADD-DD Fas-associated death domain protein",
      "SOURCE": "Homo sapiens",
      "LENGTH": 100.0,
      "UniProt": "Q13158",
      "PDB_wild": "1e41",
      "MUTATED_CHAIN": "A",
      "PFAM": [
         "PF00531"
      ],
      "CATH": [
         "1e41A00 (1.10.533.10)"
      ],
      "MUTATION_UNIPROT": "D127A",
      "MUTATION_PDB": "D127A",
      "SEC_STR": "Helix",
      "RSA": "62.0",
      "T": 25.0,
      "pH": 7.0,
      "BUFFER_NAME": "Phosphate",
      "BUFFER_CONC": "0.05",
      "ADDITIVES": "5 mM DTT",
      "MEASURE_KIN": "stopped-flow",
      "METHOD_KIN": "Urea",
      "mu": 6.28,
      "AUTHOR_KIN": "Steward A, McDowell GS ,Clarke J",
      "REFERENCE_KIN": "Topology is the Principal Determinant in the Folding of a Complex All-alpha Greek Key Death Domain from Human FADD, J Mol Biol.  389(2-3): 425\u2013437. https://doi.org/10.1016/j.jmb.2009.04.004",
      "YEAR_KIN": 2009.0,
      "PMID_KIN": "19362094",
      "STATE": "2",
      "REVERSIBILITY": "yes",
      "REVIEW_DATE": "2023-06-11T01:00:00"
   }
]