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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:4536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,536 | train | mutant | 3,648 | 55 | 4,093 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Q | W126Q | 1 | 1 | 0 | 0 | 126 | W | Q | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,378 | ProTherm | 3.5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Q | null | null | 3.43 | 3.59 | null | null | null | 1.18 | 2.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28468,"numValue":3.43,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28469,"numValue":3.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28470,"numValue":2.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28471,"numValue":1.18,"references":[],... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,537 | train | mutant | 3,648 | 55 | 4,093 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Q | W126Q | 1 | 1 | 0 | 0 | 126 | W | Q | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,380 | ProTherm | 4 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Q | null | null | 4.83 | 3.61 | null | null | null | 1.66 | 2.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28478,"numValue":4.83,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28479,"numValue":3.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28480,"numValue":2.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28481,"numValue":1.66,"references":[],... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,538 | train | mutant | 3,648 | 55 | 4,093 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Q | W126Q | 1 | 1 | 0 | 0 | 126 | W | Q | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,382 | ProTherm | 4.5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Q | null | null | 5.56 | 4 | null | null | null | 1.91 | 2.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28488,"numValue":5.56,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28489,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28490,"numValue":2.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28491,"numValue":1.91,"references":[],"... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,540 | train | mutant | 3,648 | 55 | 4,093 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W126Q | W126Q | 1 | 1 | 0 | 0 | 126 | W | Q | 9 | CONSERVATION | 4LYZ | 453 | null | 126 | A | S | true | false | 12.168413 | 6.242857 | 8,386 | ProTherm | 5.5 | Fluorescence | GdnHCl | Sodium acetate | 0.1 M | 35 | 4LYZ_A:W108Q | null | null | 5.91 | 3.44 | null | null | null | 2.03 | 2.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 571 | ARTICLE | Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. | 1,992 | 10.1021/bi00139a017 | 1610799 | Biochemistry;31;5545-53 | 5 | Kuroki R|Yamada H|Miki T|Inoue M|Yasukochi T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","t... | [{"datasets":[],"id":28508,"numValue":5.91,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28509,"numValue":3.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28510,"numValue":2.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28511,"numValue":2.03,"references":[],... | [{"id":7229,"numValue":9.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,542 | train | mutant | 595 | 55 | 646 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R132H | R132H | 1 | 1 | 0 | 0 | 132 | R | H | 4 | CONSERVATION | 4LYZ | 453 | null | 132 | A | H | false | false | 135.282136 | 6.356364 | 6,582 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | 74 | 4LYZ_A:R114H | null | null | null | -0.68 | null | 2.25 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":74.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type"... | [{"datasets":[],"id":23526,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23527,"numValue":-0.68,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23528,"numValue":null,"referen... | [{"id":7235,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,543 | train | mutant | 54 | 55 | 60 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G135A | G135A | 1 | 1 | 0 | 0 | 135 | G | A | 5 | CONSERVATION | 4LYZ | 453 | null | 135 | A | T | false | false | 81.501221 | 5.25 | 68 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 4LYZ_A:G117A | 61 | -4.6 | null | null | 110.9 | 1.53 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:G117A","type":"_P... | [{"datasets":[],"id":231,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":232,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":233,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2... | [{"id":7238,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,544 | train | mutant | 54 | 55 | 60 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G135A | G135A | 1 | 1 | 0 | 0 | 135 | G | A | 5 | CONSERVATION | 4LYZ | 453 | null | 135 | A | T | false | false | 81.501221 | 5.25 | 6,762 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 65.6 | 4LYZ_A:G117A | null | null | null | 1.46 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":65.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23994,"numValue":1.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23995,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7238,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4545 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,545 | train | mutant | 6,995 | 55 | 7,647 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G135P|T136G | G135P|T136G | 2 | 2 | 0 | 0 | 135 | G | P | 5 | CONSERVATION | 4LYZ | 453 | null | 135|136 | A | T|S | false | false | 79.278816 | 6.085 | 15,133 | ProTherm | 5.5 | Fluorescence | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:G117P 4LYZ_A:T118G | null | null | 7.2 | 2.6 | null | null | null | 2.58 | 2.8 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 572 | ARTICLE | Correlation between the differences in the free energy change and conformational energy in the folded state of hen lysozymes with Gly-Pro and Pro-Gly sequences introduced to the same site. | 1,995 | 10.1093/oxfordjournals.jbchem.a124999 | 8720127 | J Biochem;118;1138-44 | 5 | Ueda T|Motoshima H|Imoto T|Hashimoto Y|Tsutsumi M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"B... | [{"datasets":[],"id":55519,"numValue":7.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55520,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55521,"numValue":2.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55522,"numValue":2.58,"references":[],"st... | [{"id":7238,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7239,"numValue":3.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,546 | train | mutant | 3,649 | 55 | 4,094 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T136P | T136P | 1 | 1 | 0 | 0 | 136 | T | P | 3 | CONSERVATION | 4LYZ | 453 | null | 136 | A | S | false | false | 77.05641 | 6.92 | 8,387 | ProTherm | 5.5 | Fluorescence | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:T118P | null | null | 7.8 | 2 | null | null | null | 2.77 | 2.8 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 572 | ARTICLE | Correlation between the differences in the free energy change and conformational energy in the folded state of hen lysozymes with Gly-Pro and Pro-Gly sequences introduced to the same site. | 1,995 | 10.1093/oxfordjournals.jbchem.a124999 | 8720127 | J Biochem;118;1138-44 | 5 | Ueda T|Motoshima H|Imoto T|Hashimoto Y|Tsutsumi M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"B... | [{"datasets":[],"id":28513,"numValue":7.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28514,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28515,"numValue":2.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28516,"numValue":2.77,"references":[],"st... | [{"id":7239,"numValue":3.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,547 | train | mutant | 596 | 55 | 647 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q139H | Q139H | 1 | 1 | 0 | 0 | 139 | Q | H | 5 | CONSERVATION | 4LYZ | 453 | null | 139 | A | G | false | false | 112.981345 | 3.835556 | 1,011 | ProTherm | 6.4 | CD | Thermal | Potassium phosphate | 66 mM | null | 4LYZ_A:Q121H | 72.8 | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 104 | ARTICLE | Design and structural analysis of an engineered thermostable chicken lysozyme. | 1,995 | 10.1002/pro.5560041011 | 8535242 | Protein Sci;4;2063-72 | 2 | Shih P|Kirsch J F | [{"numValue":6.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"4LYZ_A:Q121H",... | [{"datasets":[],"id":3781,"numValue":72.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3782,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3783,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7242,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,549 | train | mutant | 6,996 | 55 | 7,648 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q139P|A140G | Q139P|A140G | 2 | 2 | 0 | 0 | 139 | Q | P | 5 | CONSERVATION | 4LYZ | 453 | null | 139|140 | A | G | false | false | 69.326728 | 4.701778 | 15,134 | ProTherm | 5.5 | Fluorescence | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:Q121P 4LYZ_A:A122G | null | null | 7 | 2.8 | null | null | null | 2.59 | 2.7 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 572 | ARTICLE | Correlation between the differences in the free energy change and conformational energy in the folded state of hen lysozymes with Gly-Pro and Pro-Gly sequences introduced to the same site. | 1,995 | 10.1093/oxfordjournals.jbchem.a124999 | 8720127 | J Biochem;118;1138-44 | 5 | Ueda T|Motoshima H|Imoto T|Hashimoto Y|Tsutsumi M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"B... | [{"datasets":[],"id":55524,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55525,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55526,"numValue":2.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55527,"numValue":2.59,"references":[],"st... | [{"id":7242,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7243,"numValue":3.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,550 | train | mutant | 6,997 | 55 | 7,649 | 147 | 147 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q139G|A140P | Q139G|A140P | 2 | 2 | 0 | 0 | 139 | Q | G | 5 | CONSERVATION | 4LYZ | 453 | null | 139|140 | A | G | false | false | 69.326728 | 4.701778 | 15,135 | ProTherm | 5.5 | Fluorescence | GdnHCl | acetate | 0.1 M | 35 | 4LYZ_A:Q121G 4LYZ_A:A122P | null | null | 8.1 | 1.7 | null | null | null | 2.88 | 2.8 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 572 | ARTICLE | Correlation between the differences in the free energy change and conformational energy in the folded state of hen lysozymes with Gly-Pro and Pro-Gly sequences introduced to the same site. | 1,995 | 10.1093/oxfordjournals.jbchem.a124999 | 8720127 | J Biochem;118;1138-44 | 5 | Ueda T|Motoshima H|Imoto T|Hashimoto Y|Tsutsumi M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":35.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"B... | [{"datasets":[],"id":55529,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55530,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55531,"numValue":2.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55532,"numValue":2.88,"references":[],"st... | [{"id":7242,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7243,"numValue":3.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,551 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,475 | ProTherm | 7.8 | Enzyme activity | Thermal | sodium N,N-bis(2-hydroxyethyl)glycine | 0.05 M | null | 46 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 9 | ARTICLE | Site-directed mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. | 1,988 | 10.1016/s0006-291x(88)80333-4 | 3126743 | Biochem Biophys Res Commun;151;672-8 | 5 | Ahmed S A|Kawasaki H|Bauerle R|Morita H|Miles E W | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Enzyme activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium N,N-bis(2-hydroxyethyl)glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64475,"numValue":46.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64476,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:4552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,552 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,726 | ProTherm | 9.01 | DSC | Thermal | sodium tetraborate | 1 mM | null | 46.2 | null | null | null | 3.03 | null | 3.68 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1028 | ARTICLE | -1 | DOI: 10.1016/0040-6031(90)80386-D | 4 | Yutani K|Ogasahara K|Sugisaki Y|Miles EW | [{"numValue":9.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65497,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65498,"numValue":3.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65499,"numValue":3.68,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65500,"numValue":null,"references":[... | ||||||||||||||||||||||||||||
fireprotdb:4553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,553 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,567 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 47.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(>70%) | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 379 | ARTICLE | A thermodynamic analysis of conformational change due to the alpha 2 beta 2 complex formation of tryptophan synthase. | 1,996 | 10.1111/j.1432-1033.1996.0063h.x | 8797836 | Eur J Biochem;240;63-70 | 2 | Yutani K|Hiraga K | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71989,"numValue":47.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71990,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:4554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,554 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,683 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 13.17 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":75521,"numValue":13.17,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75522,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:4555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,555 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,684 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 7.35 | null | null | null | null | 2.75 | 2.68 | null | null | null | null | null | null | null | yes | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":75523,"numValue":7.35,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75524,"numValue":2.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75525,"numValue":2.75,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75526,"numValue":3.0,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:4556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,556 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,685 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.81 | null | null | null | null | 3.64 | 1.6 | null | null | null | null | null | null | null | yes | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":75528,"numValue":5.81,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75529,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75530,"numValue":3.64,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75531,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:4557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,557 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,709 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 7.4 | null | null | null | null | 2.75 | 2.7 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":75636,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75637,"numValue":2.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75638,"numValue":2.75,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75639,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:4558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,558 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,710 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.8 | null | null | null | null | 3.63 | 1.6 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":75641,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75642,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75643,"numValue":3.63,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75644,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:4559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,559 | train | sequence | 66 | 66 | -1 | 268 | -1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,251 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | null | null | 9.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1452 | ARTICLE | Comparison of denaturation of tryptophan synthase alpha-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid. | 1,984 | 10.1016/0003-9861(84)90174-7 | 6367660 | Arch Biochem Biophys;229;448-54 | 4 | Yutani K|Sato T|Ogasahara K|Miles E W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":77324,"numValue":9.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77325,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:4560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,560 | train | mutant | 4,430 | 66 | 4,948 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18G | A18G | 1 | 1 | 0 | 0 | 18 | A | G | 8 | CONSERVATION | 2WSY | 333 | null | 18 | A|C | E | true | false | 1.034601 | 26.656 | 10,505 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18G | null | null | 3.3 | 4.1 | null | null | null | 1.88 | 1.7 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36062,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36063,"numValue":4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36064,"numValue":1.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36065,"numValue":1.88,"references":[],"st... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,561 | train | mutant | 4,431 | 66 | 4,949 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18V | A18V | 1 | 1 | 0 | 0 | 18 | A | V | 8 | CONSERVATION | 2WSY | 333 | null | 18 | A|C | E | true | false | 1.034601 | 26.656 | 10,506 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18V | null | null | 5.8 | 0 | null | null | null | 3.77 | 1.5 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36068,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36069,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36070,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36071,"numValue":3.77,"references":[],"st... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,562 | train | mutant | 4,431 | 66 | 4,949 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18V | A18V | 1 | 1 | 0 | 0 | 18 | A | V | 8 | CONSERVATION | 2WSY | 333 | null | 18 | A|C | E | true | false | 1.034601 | 26.656 | 10,507 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18V | null | null | 3.3 | 4.1 | null | null | null | 2.24 | 1.5 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36074,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36075,"numValue":4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36076,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36077,"numValue":2.24,"references":[],"st... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,564 | train | mutant | 7,090 | 66 | 7,743 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18G|I232V | A18G|I232V | 2 | 2 | 0 | 0 | 18 | A | G | 8 | CONSERVATION | 2WSY | 333 | null | 18|232 | A|C | E | true | false | 0.884563 | 26.99425 | 15,294 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18G 2WSY_A:I232V | null | null | 1.9 | 5.5 | null | null | null | 2.08 | 0.9 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":56106,"numValue":1.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56107,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56108,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56109,"numValue":2.08,"references":[],"st... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7482,"numValue":9.0,"position":232,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,565 | train | mutant | 7,090 | 66 | 7,743 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18G|I232V | A18G|I232V | 2 | 2 | 0 | 0 | 18 | A | G | 8 | CONSERVATION | 2WSY | 333 | null | 18|232 | A|C | E | true | false | 0.884563 | 26.99425 | 15,295 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18G 2WSY_A:I232V | null | null | 5.6 | 0.2 | null | null | null | 3.46 | 1.6 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":56112,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56113,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56114,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56115,"numValue":3.46,"references":[],"st... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7482,"numValue":9.0,"position":232,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,566 | train | mutant | 7,091 | 66 | 7,744 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18V|I232V | A18V|I232V | 2 | 2 | 0 | 0 | 18 | A | V | 8 | CONSERVATION | 2WSY | 333 | null | 18|232 | A|C | E | true | false | 0.884563 | 26.99425 | 15,296 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18V 2WSY_A:I232V | null | null | 4.4 | 3 | null | null | null | 2.12 | 2.1 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":56118,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56119,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56120,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56121,"numValue":2.12,"references":[],"st... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7482,"numValue":9.0,"position":232,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,567 | train | mutant | 7,091 | 66 | 7,744 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | A18V|I232V | A18V|I232V | 2 | 2 | 0 | 0 | 18 | A | V | 8 | CONSERVATION | 2WSY | 333 | null | 18|232 | A|C | E | true | false | 0.884563 | 26.99425 | 15,297 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:A18V 2WSY_A:I232V | null | null | 6.8 | -1 | null | null | null | 3.73 | 1.8 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":56124,"numValue":6.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56125,"numValue":-1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56126,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56127,"numValue":3.73,"references":[],"s... | [{"id":7268,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7482,"numValue":9.0,"position":232,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,568 | train | mutant | 4,343 | 66 | 4,853 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22L | F22L | 1 | 1 | 0 | 0 | 22 | F | L | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,289 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22L | null | null | 12.11 | 1.05 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35254,"numValue":12.11,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35255,"numValue":1.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35256,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,569 | train | mutant | 4,343 | 66 | 4,853 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22L | F22L | 1 | 1 | 0 | 0 | 22 | F | L | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,292 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22L | null | null | 6.38 | 0.97 | null | null | null | 2.1 | 2.96 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35263,"numValue":6.38,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35264,"numValue":0.97,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35265,"numValue":2.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35266,"numValue":2.1,"references":[],"... | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,570 | train | mutant | 4,343 | 66 | 4,853 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22L | F22L | 1 | 1 | 0 | 0 | 22 | F | L | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,293 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22L | null | null | 5.73 | 0.08 | null | null | null | 3.3 | 1.7 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35269,"numValue":5.73,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35270,"numValue":0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35271,"numValue":1.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35272,"numValue":3.3,"references":[],"s... | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,571 | train | mutant | 4,344 | 66 | 4,854 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22I | F22I | 1 | 1 | 0 | 0 | 22 | F | I | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,290 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22I | null | null | 8.58 | 4.58 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35257,"numValue":8.58,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35258,"numValue":4.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35259,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,572 | train | mutant | 4,344 | 66 | 4,854 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22I | F22I | 1 | 1 | 0 | 0 | 22 | F | I | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,294 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22I | null | null | 3.16 | 4.19 | null | null | null | 2 | 1.57 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35275,"numValue":3.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35276,"numValue":4.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35277,"numValue":1.57,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35278,"numValue":2.0,"references":[],"... | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,573 | train | mutant | 4,344 | 66 | 4,854 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22I | F22I | 1 | 1 | 0 | 0 | 22 | F | I | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,295 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22I | null | null | 5.43 | 0.38 | null | null | null | 3.6 | 1.51 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35281,"numValue":5.43,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35282,"numValue":0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35283,"numValue":1.51,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35284,"numValue":3.6,"references":[],"... | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,574 | train | mutant | 4,345 | 66 | 4,855 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22V | F22V | 1 | 1 | 0 | 0 | 22 | F | V | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,291 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22V | null | null | 9.72 | 3.44 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35260,"numValue":9.72,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35261,"numValue":3.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35262,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:4576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,576 | train | mutant | 4,345 | 66 | 4,855 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | F22V | F22V | 1 | 1 | 0 | 0 | 22 | F | V | 8 | CONSERVATION | 2WSY | 333 | null | 22 | A|C | E | true | false | 13.479459 | 24.617273 | 10,297 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:F22V | null | null | 5.87 | -0.06 | null | null | null | 3.3 | 1.74 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 669 | ARTICLE | Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. | 1,992 | 10.1021/bi00123a002 | 1540577 | Biochemistry;31;2219-23 | 3 | Chen X|Matthews C R|Rambo R | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":35293,"numValue":5.87,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35294,"numValue":-0.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35295,"numValue":1.74,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35296,"numValue":3.3,"references":[],... | [{"id":7272,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,578 | train | mutant | 61 | 66 | 68 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | C118S | C118S | 1 | 1 | 0 | 0 | 118 | C | S | 7 | CONSERVATION | 2WSY | 333 | null | 118 | A|C | H | false | false | 0 | 22.883333 | 80 | ProTherm | 7.8 | Enzyme activity | Thermal | sodium N,N-bis(2-hydroxyethyl)glycine | 0.05 M | null | 2WSY_A:C118S | 41 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 9 | ARTICLE | Site-directed mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. | 1,988 | 10.1016/s0006-291x(88)80333-4 | 3126743 | Biochem Biophys Res Commun;151;672-8 | 5 | Ahmed S A|Kawasaki H|Bauerle R|Morita H|Miles E W | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Enzyme activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium N,N-bis(2-hydroxyethyl)glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue"... | [{"datasets":[],"id":269,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["Saraboji_S1791.csv"],"id":270,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":271,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7368,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,579 | train | mutant | 4,434 | 66 | 4,952 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | Y175Q | Y175Q | 1 | 1 | 0 | 0 | 175 | Y | Q | 9 | CONSERVATION | 2WSY | 333 | null | 175 | A|C | E | true | false | 35.034237 | 16.004167 | 10,513 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:Y175Q | null | null | 6 | 1.4 | null | null | null | 2.05 | 2.9 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36110,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36111,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36112,"numValue":2.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36113,"numValue":2.05,"references":[],"st... | [{"id":7425,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,580 | train | mutant | 4,434 | 66 | 4,952 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | Y175Q | Y175Q | 1 | 1 | 0 | 0 | 175 | Y | Q | 9 | CONSERVATION | 2WSY | 333 | null | 175 | A|C | E | true | false | 35.034237 | 16.004167 | 10,514 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:Y175Q | null | null | 7.9 | -2.1 | null | null | null | 2.91 | 2.7 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36116,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":36117,"numValue":-2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36118,"numValue":2.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36119,... | [{"id":7425,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:4581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,581 | train | mutant | 7,092 | 66 | 7,745 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | Y175Q|L209V | Y175Q|L209V | 2 | 2 | 0 | 0 | 175 | Y | Q | 9 | CONSERVATION | 2WSY | 333 | null | 175|209 | A|C | E | true | false | 17.920231 | 16.795208 | 15,298 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:Y175Q 2WSY_A:L209V | null | null | 3.6 | 3.8 | null | null | null | 2.23 | 1.6 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":56130,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56131,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56132,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56133,"numValue":2.23,"references":[],"st... | [{"id":7425,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7459,"numValue":7.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,582 | train | mutant | 7,092 | 66 | 7,745 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | Y175Q|L209V | Y175Q|L209V | 2 | 2 | 0 | 0 | 175 | Y | Q | 9 | CONSERVATION | 2WSY | 333 | null | 175|209 | A|C | E | true | false | 17.920231 | 16.795208 | 15,299 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:Y175Q 2WSY_A:L209V | null | null | 9.7 | -3.9 | null | null | null | 4.32 | 2.2 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":56136,"numValue":9.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56137,"numValue":-3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56138,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56139,"numValue":4.32,"references":[],"s... | [{"id":7425,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7459,"numValue":7.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,583 | train | mutant | 4,433 | 66 | 4,951 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | L209V | L209V | 1 | 1 | 0 | 0 | 209 | L | V | 7 | CONSERVATION | 2WSY | 333 | null | 209 | A|C | E | true | false | 0.806226 | 17.58625 | 10,511 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:L209V | null | null | 4 | 3.4 | null | null | null | 2.3 | 1.7 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36098,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36099,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36100,"numValue":1.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36101,"numValue":2.3,"references":[],"str... | [{"id":7459,"numValue":7.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,584 | train | mutant | 4,433 | 66 | 4,951 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | L209V | L209V | 1 | 1 | 0 | 0 | 209 | L | V | 7 | CONSERVATION | 2WSY | 333 | null | 209 | A|C | E | true | false | 0.806226 | 17.58625 | 10,512 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:L209V | null | null | 3.8 | 2 | null | null | null | 3.44 | 1.1 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36104,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36105,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36106,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36107,"numValue":3.44,"references":[],"st... | [{"id":7459,"numValue":7.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,585 | train | mutant | 4,432 | 66 | 4,950 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | I232V | I232V | 1 | 1 | 0 | 0 | 232 | I | V | 9 | CONSERVATION | 2WSY | 333 | null | 232 | A|C | E | true | false | 0.734524 | 27.3325 | 10,509 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:I232V | null | null | 3.5 | 3.9 | null | null | null | 2.31 | 1.5 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36086,"numValue":3.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36087,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36088,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36089,"numValue":2.31,"references":[],"st... | [{"id":7482,"numValue":9.0,"position":232,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,586 | train | mutant | 4,432 | 66 | 4,950 | 268 | 268 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | 7 | Tryptophan synthase alpha chain | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) | 1 | P00929 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | I232V | I232V | 1 | 1 | 0 | 0 | 232 | I | V | 9 | CONSERVATION | 2WSY | 333 | null | 232 | A|C | E | true | false | 0.734524 | 27.3325 | 10,510 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 2WSY_A:I232V | null | null | 4.3 | 1.5 | null | null | null | 3.28 | 1.3 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 683 | ARTICLE | Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. | 1,993 | 10.1021/bi00072a011 | 8504078 | Biochemistry;32;5566-75 | 4 | Chen X|Matthews C R|Chrunyk B A|Tsuji T | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":36092,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36093,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36094,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36095,"numValue":3.28,"references":[],"st... | [{"id":7482,"numValue":9.0,"position":232,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:4587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,587 | train | sequence | 69 | 69 | -1 | 68 | -1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,084 | ProTherm | 2.5 | DSC | Thermal | dialyzate | null | 70.9 | null | null | null | 64 | 0.42 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 10 | ARTICLE | Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V. | 2,001 | 10.1110/ps.26801 | 11266603 | Protein Sci;10;149-60 | 6 | Zavodszky M|Zolkiewski M|Wen L|Chen C W|Huang J K|Krishnamoorthi R | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"dialyzate","type":"BUFFER"}] | [{"datasets":[],"id":79956,"numValue":70.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":79957,"numValue":64.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":79958,"numValue":0.42,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":79959,"numValue":null,"references":[]... | |||||||||||||||||||||||||||
fireprotdb:4588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,588 | train | mutant | 4,889,221 | 69 | 4,895,802 | 68 | 67 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | delS1 | delS1 | 1 | 0 | 1 | 0 | 1 | S | - | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,726 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.882125 | 0.19125 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076134,"numValue":-0.88212493353374,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076135,"numValue":0.19125037767673,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,589 | train | mutant | 4,889,221 | 69 | 4,895,802 | 68 | 67 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | delS1 | delS1 | 1 | 0 | 1 | 0 | 1 | S | - | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,742 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.062326 | 0.173049 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076166,"numValue":-1.06232575142351,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076167,"numValue":0.173048732877202,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,590 | train | mutant | 4,889,222 | 69 | 4,895,803 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1A | S1A | 1 | 1 | 0 | 0 | 1 | S | A | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,727 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.026704 | 0.06344 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076136,"numValue":-0.0267042266655911,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076137,"numValue":0.0634396861833577,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,591 | train | mutant | 4,889,223 | 69 | 4,895,804 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1C | S1C | 1 | 1 | 0 | 0 | 1 | S | C | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,728 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.071733 | 0.049828 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076138,"numValue":-0.0717334439118515,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076139,"numValue":0.0498280428907811,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,592 | train | mutant | 4,889,224 | 69 | 4,895,805 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1D | S1D | 1 | 1 | 0 | 0 | 1 | S | D | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,729 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.027004 | 0.157547 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076140,"numValue":-0.0270038192631129,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076141,"numValue":0.157546930197504,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,593 | train | mutant | 4,889,225 | 69 | 4,895,806 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1E | S1E | 1 | 1 | 0 | 0 | 1 | S | E | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,730 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.125965 | 0.14378 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076142,"numValue":0.125964742257128,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076143,"numValue":0.143780155518769,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,594 | train | mutant | 4,889,226 | 69 | 4,895,807 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1F | S1F | 1 | 1 | 0 | 0 | 1 | S | F | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,731 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.017807 | 0.071267 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076144,"numValue":-0.0178073161644109,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076145,"numValue":0.0712674649630213,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,595 | train | mutant | 4,889,227 | 69 | 4,895,808 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1G | S1G | 1 | 1 | 0 | 0 | 1 | S | G | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,732 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.039613 | 0.042239 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076146,"numValue":0.0396127990056591,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076147,"numValue":0.0422393084149059,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,596 | train | mutant | 4,889,228 | 69 | 4,895,809 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1H | S1H | 1 | 1 | 0 | 0 | 1 | S | H | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,733 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.493157 | 0.120027 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076148,"numValue":-0.493157395490188,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076149,"numValue":0.120026511083906,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,597 | train | mutant | 4,889,229 | 69 | 4,895,810 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1I | S1I | 1 | 1 | 0 | 0 | 1 | S | I | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,734 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.062096 | 0.153426 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076150,"numValue":0.062095738981844,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076151,"numValue":0.15342586757826,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,598 | train | mutant | 4,889,230 | 69 | 4,895,811 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1K | S1K | 1 | 1 | 0 | 0 | 1 | S | K | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,735 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.032808 | 0.071957 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076152,"numValue":0.0328076386223113,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076153,"numValue":0.0719568248308866,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,599 | train | mutant | 4,889,231 | 69 | 4,895,812 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1L | S1L | 1 | 1 | 0 | 0 | 1 | S | L | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,736 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.285337 | 0.05198 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076154,"numValue":-0.285336578234852,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076155,"numValue":0.0519801973539516,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,600 | train | mutant | 4,889,232 | 69 | 4,895,813 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1M | S1M | 1 | 1 | 0 | 0 | 1 | S | M | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,737 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.110644 | 0.073005 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076156,"numValue":0.110644134619895,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076157,"numValue":0.0730048861060549,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,601 | train | mutant | 4,889,233 | 69 | 4,895,814 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1N | S1N | 1 | 1 | 0 | 0 | 1 | S | N | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,738 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.029649 | 0.079117 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076158,"numValue":0.0296488710250169,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076159,"numValue":0.0791172048697285,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,602 | train | mutant | 4,889,234 | 69 | 4,895,815 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1P | S1P | 1 | 1 | 0 | 0 | 1 | S | P | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,739 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.485514 | 0.099622 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076160,"numValue":-0.485513915640261,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076161,"numValue":0.0996222759022382,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,603 | train | mutant | 4,889,235 | 69 | 4,895,816 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1Q | S1Q | 1 | 1 | 0 | 0 | 1 | S | Q | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,041,740 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.136199 | 0.124868 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076162,"numValue":-0.136198843382022,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076163,"numValue":0.124867765517914,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,605 | train | mutant | 4,890,563 | 69 | 4,897,144 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1T | S1T | 1 | 1 | 0 | 0 | 1 | S | T | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,043,081 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.032576 | 0.060526 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078844,"numValue":0.0325755218350421,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078845,"numValue":0.0605259637385769,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,606 | train | mutant | 4,890,564 | 69 | 4,897,145 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1V | S1V | 1 | 1 | 0 | 0 | 1 | S | V | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,043,082 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.042458 | 0.05621 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078846,"numValue":0.0424575791659111,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078847,"numValue":0.056210183924493,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,607 | train | mutant | 4,890,565 | 69 | 4,897,146 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1W | S1W | 1 | 1 | 0 | 0 | 1 | S | W | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,043,083 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.514203 | 0.060783 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078848,"numValue":-0.514202920772497,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078849,"numValue":0.0607831815272601,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,608 | train | mutant | 4,890,566 | 69 | 4,897,147 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S1Y | S1Y | 1 | 1 | 0 | 0 | 1 | S | Y | 9 | CONSERVATION | 1TIN | 58 | null | 1 | A | L | false | false | 174.653869 | 2.319091 | 5,043,084 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.112148 | 0.109088 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078850,"numValue":-0.112147675607818,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078851,"numValue":0.10908751266124,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7519,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,609 | train | mutant | 4,889,237 | 69 | 4,895,818 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2A | S2A | 1 | 1 | 0 | 0 | 2 | S | A | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,743 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.112682 | 0.044262 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076168,"numValue":-0.112681724154031,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076169,"numValue":0.0442624941127468,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,612 | train | mutant | 4,889,240 | 69 | 4,895,821 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2E | S2E | 1 | 1 | 0 | 0 | 2 | S | E | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,746 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.105851 | 0.075224 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076174,"numValue":-0.105851102898281,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076175,"numValue":0.0752236526891068,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,613 | train | mutant | 4,889,241 | 69 | 4,895,822 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2F | S2F | 1 | 1 | 0 | 0 | 2 | S | F | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,747 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.214732 | 0.057548 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076176,"numValue":0.214732319515642,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076177,"numValue":0.057548292219226,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,614 | train | mutant | 4,889,242 | 69 | 4,895,823 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2G | S2G | 1 | 1 | 0 | 0 | 2 | S | G | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,748 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.36381 | 0.054894 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076178,"numValue":-0.363810135848968,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076179,"numValue":0.0548936229051672,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,615 | train | mutant | 4,889,243 | 69 | 4,895,824 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2H | S2H | 1 | 1 | 0 | 0 | 2 | S | H | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,749 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.212604 | 0.070063 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076180,"numValue":0.212603682621538,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076181,"numValue":0.0700626618790234,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,616 | train | mutant | 4,889,244 | 69 | 4,895,825 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2I | S2I | 1 | 1 | 0 | 0 | 2 | S | I | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,750 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.178407 | 0.064702 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076182,"numValue":0.178406941985492,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076183,"numValue":0.0647018616996198,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,617 | train | mutant | 4,889,245 | 69 | 4,895,826 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2K | S2K | 1 | 1 | 0 | 0 | 2 | S | K | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,751 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.075755 | 0.075804 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076184,"numValue":-0.0757545523641748,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076185,"numValue":0.075804475466987,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,618 | train | mutant | 4,889,246 | 69 | 4,895,827 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2L | S2L | 1 | 1 | 0 | 0 | 2 | S | L | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,752 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.065782 | 0.044601 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076186,"numValue":-0.0657815376410852,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076187,"numValue":0.0446014296060332,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,619 | train | mutant | 4,889,247 | 69 | 4,895,828 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2M | S2M | 1 | 1 | 0 | 0 | 2 | S | M | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,753 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.159651 | 0.062908 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076188,"numValue":-0.159650735993435,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076189,"numValue":0.0629076349211282,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,620 | train | mutant | 4,889,248 | 69 | 4,895,829 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2N | S2N | 1 | 1 | 0 | 0 | 2 | S | N | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,754 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.292848 | 0.087216 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076190,"numValue":0.292847715528937,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076191,"numValue":0.087215597635604,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,621 | train | mutant | 4,889,249 | 69 | 4,895,830 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2P | S2P | 1 | 1 | 0 | 0 | 2 | S | P | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,755 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.041911 | 0.046424 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076192,"numValue":-0.0419105752641297,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076193,"numValue":0.0464243650925937,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,623 | train | mutant | 4,889,251 | 69 | 4,895,832 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2R | S2R | 1 | 1 | 0 | 0 | 2 | S | R | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,041,757 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.085394 | 0.045044 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076196,"numValue":-0.0853938767136283,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076197,"numValue":0.0450444038019546,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,626 | train | mutant | 4,890,561 | 69 | 4,897,142 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2W | S2W | 1 | 1 | 0 | 0 | 2 | S | W | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,043,079 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.091912 | 0.054474 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078840,"numValue":-0.0919118600485408,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078841,"numValue":0.054474184271862,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,627 | train | mutant | 4,890,562 | 69 | 4,897,143 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | S2Y | S2Y | 1 | 1 | 0 | 0 | 2 | S | Y | 2 | CONSERVATION | 1TIN | 58 | null | 2 | A | L | true | false | 71.178323 | 1.571818 | 5,043,080 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.132655 | 0.058738 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078842,"numValue":0.132654743924311,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078843,"numValue":0.0587384665475612,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7520,"numValue":2.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,628 | train | mutant | 7,289 | 69 | 7,959 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3S|C48S | C3S|C48S | 2 | 2 | 0 | 0 | 3 | C | S | 8 | CONSERVATION | 1TIN | 58 | null | 3|48 | A | L|T | true | false | 42.835312 | 0.6385 | 15,646 | ProTherm | 2.5 | DSC | Thermal | dialyzate | null | 1TIN_A:C3S 1TIN_A:C48S | 49.2 | -21.7 | null | null | 50 | 0.59 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 10 | ARTICLE | Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V. | 2,001 | 10.1110/ps.26801 | 11266603 | Protein Sci;10;149-60 | 6 | Zavodszky M|Zolkiewski M|Wen L|Chen C W|Huang J K|Krishnamoorthi R | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"dialyzate","type":"BUFFER"},{"numValue":null,"strValue":"1TIN_A:C3S 1TIN_A:C48S","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":57419,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57420,"numValue":-21.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57421,"numValue":50.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57422,"numValue":0.59,"references":[... | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7566,"numValue":6.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:4629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,629 | train | mutant | 4,889,252 | 69 | 4,895,833 | 68 | 67 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | delC3 | delC3 | 1 | 0 | 1 | 0 | 3 | C | - | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,041,758 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.816019 | 0.103355 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076198,"numValue":-0.816019071161482,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076199,"numValue":0.103354947757668,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,630 | train | mutant | 4,889,253 | 69 | 4,895,834 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3A | C3A | 1 | 1 | 0 | 0 | 3 | C | A | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,041,759 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.051051 | 0.037777 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12076200,"numValue":0.0510512983596894,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12076201,"numValue":0.0377769891345025,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,631 | train | mutant | 4,890,541 | 69 | 4,897,122 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3D | C3D | 1 | 1 | 0 | 0 | 3 | C | D | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,059 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.297141 | 0.070372 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078800,"numValue":0.297140976415946,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078801,"numValue":0.0703722768835614,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4632 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,632 | train | mutant | 4,890,542 | 69 | 4,897,123 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3E | C3E | 1 | 1 | 0 | 0 | 3 | C | E | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,060 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.419445 | 0.064337 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078802,"numValue":-0.419444661144259,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078803,"numValue":0.0643366466274336,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,633 | train | mutant | 4,890,543 | 69 | 4,897,124 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3F | C3F | 1 | 1 | 0 | 0 | 3 | C | F | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,061 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.186786 | 0.073884 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078804,"numValue":0.186785638263932,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078805,"numValue":0.0738838350071807,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,634 | train | mutant | 4,890,544 | 69 | 4,897,125 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3G | C3G | 1 | 1 | 0 | 0 | 3 | C | G | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,062 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.10221 | 0.033779 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078806,"numValue":-0.102209568370566,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078807,"numValue":0.0337793532673725,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,635 | train | mutant | 4,890,545 | 69 | 4,897,126 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3H | C3H | 1 | 1 | 0 | 0 | 3 | C | H | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,063 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.102916 | 0.079757 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078808,"numValue":0.102915905152291,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078809,"numValue":0.079757406360631,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,636 | train | mutant | 4,890,546 | 69 | 4,897,127 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3I | C3I | 1 | 1 | 0 | 0 | 3 | C | I | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,064 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.191033 | 0.074254 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078810,"numValue":0.191033015599969,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078811,"numValue":0.0742537104086617,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,637 | train | mutant | 4,890,547 | 69 | 4,897,128 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3K | C3K | 1 | 1 | 0 | 0 | 3 | C | K | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,065 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.040126 | 0.056117 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078812,"numValue":0.0401256151635793,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078813,"numValue":0.0561173821934588,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,638 | train | mutant | 4,890,548 | 69 | 4,897,129 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3L | C3L | 1 | 1 | 0 | 0 | 3 | C | L | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,066 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.175579 | 0.035924 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078814,"numValue":0.175579255697171,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078815,"numValue":0.0359241843559369,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,639 | train | mutant | 4,890,549 | 69 | 4,897,130 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3M | C3M | 1 | 1 | 0 | 0 | 3 | C | M | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,067 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.00419 | 0.052549 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078816,"numValue":-0.00418979797795491,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078817,"numValue":0.0525489374634092,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,640 | train | mutant | 4,890,550 | 69 | 4,897,131 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3N | C3N | 1 | 1 | 0 | 0 | 3 | C | N | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,068 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.210957 | 0.073895 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078818,"numValue":0.210957272851373,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078819,"numValue":0.0738948920432874,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,641 | train | mutant | 4,890,551 | 69 | 4,897,132 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3P | C3P | 1 | 1 | 0 | 0 | 3 | C | P | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,069 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.108839 | 0.045689 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078820,"numValue":0.108839381615004,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078821,"numValue":0.0456894815447447,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,642 | train | mutant | 4,890,552 | 69 | 4,897,133 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3Q | C3Q | 1 | 1 | 0 | 0 | 3 | C | Q | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,070 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.0127 | 0.055217 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078822,"numValue":0.0126998471670199,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078823,"numValue":0.0552166521007835,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,643 | train | mutant | 4,890,553 | 69 | 4,897,134 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3R | C3R | 1 | 1 | 0 | 0 | 3 | C | R | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,071 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.031391 | 0.03328 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078824,"numValue":-0.0313906466070056,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078825,"numValue":0.0332803381618426,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,645 | train | mutant | 4,890,555 | 69 | 4,897,136 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3T | C3T | 1 | 1 | 0 | 0 | 3 | C | T | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,073 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.111706 | 0.041377 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078828,"numValue":0.111705754034537,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078829,"numValue":0.0413771924792444,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,646 | train | mutant | 4,890,556 | 69 | 4,897,137 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3V | C3V | 1 | 1 | 0 | 0 | 3 | C | V | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,074 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.115026 | 0.033972 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078830,"numValue":0.115025563898967,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078831,"numValue":0.0339720731782288,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,647 | train | mutant | 4,890,557 | 69 | 4,897,138 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3W | C3W | 1 | 1 | 0 | 0 | 3 | C | W | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,075 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.250953 | 0.053358 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078832,"numValue":-0.250952524749545,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078833,"numValue":0.0533579364412397,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:4648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4,648 | train | mutant | 4,890,558 | 69 | 4,897,139 | 68 | 68 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | 8 | Inhibitor of trypsin and hageman factor | Cucurbita maxima | 1 | P19873 | IPR000864|IPR036354 | C3Y | C3Y | 1 | 1 | 0 | 0 | 3 | C | Y | 8 | CONSERVATION | 1TIN | 58 | null | 3 | A | L | true | false | 48.754777 | 0.733 | 5,043,076 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.177583 | 0.047898 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12078834,"numValue":0.17758283742294,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12078835,"numValue":0.0478984056562744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":7521,"numValue":8.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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