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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:2990 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,990 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 625 | ProTherm | 3 | CD | Thermal | HCl | null | 2LZM_A:T157I | 40.6 | -11 | 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|_PDB_CHAIN_MUTATION | 68 | ARTICLE | Structure and thermal stability of phage T4 lysozyme. | 1,987 | 10.1016/0076-6879(87)54093-9 | 3323816 | Methods Enzymol;154;511-33 | 2 | Alber T|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:T157I","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2481,"numValue":40.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2482,"numValue":-11.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2483,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2991 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,991 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 638 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157I | 31 | -11 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2520,"numValue":31.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2521,"numValue":-11.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2522,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2992 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,992 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 689 | ProTherm | 4 | CD | Thermal | Sodium acetate | 20 mM | null | KCl | 0.2 M | 2LZM_A:T157I | 57 | -5.8 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 76 | ARTICLE | Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile. | 1,987 | 10.1016/0022-2836(87)90126-4 | 3681997 | J Mol Biol;197;315-29 | 5 | Matthews B W|Gr?tter M G|Gray T M|Weaver L H|Wilson T A | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},... | [{"datasets":[],"id":2690,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2691,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2692,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2993 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,993 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 690 | ProTherm | 6 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:T157I | 61.5 | -3 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 76 | ARTICLE | Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile. | 1,987 | 10.1016/0022-2836(87)90126-4 | 3681997 | J Mol Biol;197;315-29 | 5 | Matthews B W|Gr?tter M G|Gray T M|Weaver L H|Wilson T A | [{"numValue":6.0,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":2693,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2694,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2695,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2994 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,994 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 856 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157I | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3225,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3226,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2995 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,995 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 863 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157I | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3239,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3240,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2996 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,996 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 870 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157I | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3253,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3254,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2997 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,997 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,020 | ProTherm | 6 | CD | Thermal | Potassium phosphate | 20 mM | 64.5 | KCl | 0.2 M | 2LZM_A:T157I | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 76 | ARTICLE | Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile. | 1,987 | 10.1016/0022-2836(87)90126-4 | 3681997 | J Mol Biol;197;315-29 | 5 | Matthews B W|Gr?tter M G|Gray T M|Weaver L H|Wilson T A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":64.5,"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":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24700,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24701,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2998 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,998 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,060 | ProTherm | 4 | CD | Thermal | Sodium acetate | 20 mM | 62.8 | KCl | 0.2 M | 2LZM_A:T157I | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 76 | ARTICLE | Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile. | 1,987 | 10.1016/0022-2836(87)90126-4 | 3681997 | J Mol Biol;197;315-29 | 5 | Matthews B W|Gr?tter M G|Gray T M|Weaver L H|Wilson T A | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":62.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":24792,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24793,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2999 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,999 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,323 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157I | null | null | null | 1.5 | null | 3.11 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25550,"numValue":3.11,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25551,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25552,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3001 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,001 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,028 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157I | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27369,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27370,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3002 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,002 | train | mutant | 362 | 41 | 401 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157I | T157I | 1 | 1 | 0 | 0 | 157 | T | I | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,205 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157I | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv"],"id":27800,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27801,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3003 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,003 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 626 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157N | 40.3 | -1.7 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2484,"numValue":40.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2485,"numValue":-1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2486,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3004 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,004 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 858 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157N | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3229,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3230,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3006 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,006 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 872 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157N | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3257,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3258,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3007 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,007 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,325 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157N | null | null | null | 1.2 | null | 3.37 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25556,"numValue":3.37,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25557,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25558,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3008 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,008 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,843 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.2 | KCl | 25 mM | 2LZM_A:T157N | null | null | null | 1.1 | null | 3.37 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26831,"numValue":3.37,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26832,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26833,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3009 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,009 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,016 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157N | null | null | null | 0.45 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27345,"numValue":0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27346,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3010 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,010 | train | mutant | 363 | 41 | 402 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157N | T157N | 1 | 1 | 0 | 0 | 157 | T | N | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,207 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157N | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27804,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27805,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3011 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,011 | train | mutant | 364 | 41 | 403 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157S | T157S | 1 | 1 | 0 | 0 | 157 | T | S | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 627 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157S | 39.5 | -2.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":2487,"numValue":39.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":2488,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"da... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3012 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,012 | train | mutant | 364 | 41 | 403 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157S | T157S | 1 | 1 | 0 | 0 | 157 | T | S | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,017 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157S | null | null | null | 0.66 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27347,"numValue":0.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27348,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3013 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,013 | train | mutant | 365 | 41 | 404 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157D | T157D | 1 | 1 | 0 | 0 | 157 | T | D | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 628 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157D | 37.8 | -4.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":2490,"numValue":37.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2491,"numValue":-4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2492,"numValue":null,"references":[],"strVal... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3014 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,014 | train | mutant | 365 | 41 | 404 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157D | T157D | 1 | 1 | 0 | 0 | 157 | T | D | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,018 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157D | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27349,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27350,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3015 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,015 | train | mutant | 365 | 41 | 404 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157D | T157D | 1 | 1 | 0 | 0 | 157 | T | D | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 12,625 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:T157D | null | null | null | 2.39 | null | null | null | 5.1 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["SAAFEC_S1262.csv"],"id":45778,"numValue":2.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45779,"numValue":5.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45780,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3016 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,016 | train | mutant | 366 | 41 | 405 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157G | T157G | 1 | 1 | 0 | 0 | 157 | T | G | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 629 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157G | 37.8 | -4.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":2493,"numValue":37.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2494,"numValue":-4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2495,"numValue":null,"refe... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3017 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,017 | train | mutant | 366 | 41 | 405 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157G | T157G | 1 | 1 | 0 | 0 | 157 | T | G | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,019 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157G | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27351,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27352,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3018 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,018 | train | mutant | 367 | 41 | 406 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157C | T157C | 1 | 1 | 0 | 0 | 157 | T | C | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 630 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157C | 37.1 | -4.9 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2496,"numValue":37.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2497,"numValue":-4.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2498,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3019 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,019 | train | mutant | 367 | 41 | 406 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157C | T157C | 1 | 1 | 0 | 0 | 157 | T | C | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,020 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157C | null | null | null | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27353,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27354,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3020 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,020 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 631 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157L | 37 | -5 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2499,"numValue":37.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2500,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2501,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3021 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,021 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 857 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157L | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3227,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3228,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3022 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,022 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 864 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157L | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3241,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3242,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3023 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,023 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 871 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157L | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3255,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3256,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3024 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,024 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,324 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157L | null | null | null | 1.7 | null | 1.74 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25553,"numValue":1.74,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25554,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25555,"numValue":null,"references":[],"strValue":"yes","type":"R... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3026 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,026 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,021 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157L | null | null | null | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27355,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27356,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3027 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,027 | train | mutant | 368 | 41 | 407 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157L | T157L | 1 | 1 | 0 | 0 | 157 | T | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,206 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157L | null | null | null | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27802,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27803,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3028 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,028 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 632 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157R | 36.9 | -5.1 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2502,"numValue":36.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2503,"numValue":-5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2504,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3029 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,029 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 859 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157R | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3231,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3232,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3030 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,030 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 866 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157R | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3245,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3246,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3032 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,032 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,326 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157R | null | null | null | -0.3 | null | 2.65 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25559,"numValue":2.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25560,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25561,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3033 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,033 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,844 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.2 | KCl | 25 mM | 2LZM_A:T157R | null | null | null | 0.6 | null | 2.65 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26834,"numValue":2.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26835,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26836,"numValue":null,"references":[],"strValue":"yes","type":"R... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3034 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,034 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,022 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157R | null | null | null | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27357,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27358,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3035 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,035 | train | mutant | 369 | 41 | 408 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157R | T157R | 1 | 1 | 0 | 0 | 157 | T | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,208 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157R | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv"],"id":27806,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27807,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3036 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,036 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 633 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157A | 36.6 | -5.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2505,"numValue":36.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2506,"numValue":-5.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":2507,"numValue":null,"refe... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3037 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,037 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 854 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157A | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3221,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3222,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3038 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,038 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 861 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157A | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3235,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3236,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3039 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,039 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 868 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157A | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3249,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3250,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3040 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,040 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,321 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157A | null | null | null | 0.5 | null | 2.43 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25544,"numValue":2.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25545,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25546,"num... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3042 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,042 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,023 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157A | null | null | null | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27359,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27360,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3043 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,043 | train | mutant | 370 | 41 | 409 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157A | T157A | 1 | 1 | 0 | 0 | 157 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,203 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157A | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv"],"id":27796,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27797,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3044 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,044 | train | mutant | 371 | 41 | 410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157E | T157E | 1 | 1 | 0 | 0 | 157 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 634 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157E | 36.2 | -5.8 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2508,"numValue":36.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2509,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2510,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3045 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,045 | train | mutant | 371 | 41 | 410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157E | T157E | 1 | 1 | 0 | 0 | 157 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 855 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157E | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3223,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3224,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3047 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,047 | train | mutant | 371 | 41 | 410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157E | T157E | 1 | 1 | 0 | 0 | 157 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 869 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157E | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3251,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3252,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3048 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,048 | train | mutant | 371 | 41 | 410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157E | T157E | 1 | 1 | 0 | 0 | 157 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,322 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157E | null | null | null | 0.8 | null | 2.3 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25547,"numValue":2.3,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25548,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25549,"numValue":null,"references":[],"strValue":"yes","type":"REVER... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3050 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,050 | train | mutant | 371 | 41 | 410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157E | T157E | 1 | 1 | 0 | 0 | 157 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,024 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157E | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27361,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27362,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3051 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,051 | train | mutant | 371 | 41 | 410 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157E | T157E | 1 | 1 | 0 | 0 | 157 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,204 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157E | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv"],"id":27798,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27799,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3052 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,052 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 635 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157V | 36 | -6 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2511,"numValue":36.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2512,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2513,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3053 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,053 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 860 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157V | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3233,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3234,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3054 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,054 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 867 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157V | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3247,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3248,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3055 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,055 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 874 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:T157V | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3261,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3262,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3056 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,056 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,327 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:T157V | null | null | null | 1.2 | null | 2.45 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":25562,"numValue":2.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25563,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25564,"num... | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3057 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,057 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 7,845 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.2 | KCl | 25 mM | 2LZM_A:T157V | null | null | null | 1.6 | null | 2.45 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26837,"numValue":2.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26838,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26839,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3058 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,058 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,025 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157V | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27363,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27364,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3059 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,059 | train | mutant | 372 | 41 | 411 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157V | T157V | 1 | 1 | 0 | 0 | 157 | T | V | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,209 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:T157V | null | null | null | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 94 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. | 1,991 | 10.1021/bi00221a022 | 1993203 | Biochemistry;30;1887-91 | 6 | Kitamura S|Connelly P|Ghosaini L|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv"],"id":27808,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27809,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3060 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,060 | train | mutant | 373 | 41 | 412 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157H | T157H | 1 | 1 | 0 | 0 | 157 | T | H | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 636 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157H | 34.1 | -7.9 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2514,"numValue":34.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2515,"numValue":-7.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2516,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3061 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,061 | train | mutant | 373 | 41 | 412 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157H | T157H | 1 | 1 | 0 | 0 | 157 | T | H | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,026 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157H | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27365,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27366,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3062 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,062 | train | mutant | 374 | 41 | 413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157F | T157F | 1 | 1 | 0 | 0 | 157 | T | F | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 637 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:T157F | 32.8 | -9.2 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2517,"numValue":32.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2518,"numValue":-9.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2519,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3063 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,063 | train | mutant | 374 | 41 | 413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157F | T157F | 1 | 1 | 0 | 0 | 157 | T | F | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 8,027 | ProTherm | 2 | CD | Thermal | Unknown | 42 | KCl | 0.2 M | 2LZM_A:T157F | null | null | null | 2.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 69 | ARTICLE | Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. | 1,987 | 10.1038/330041a0 | 3118211 | Nature;330;41-6 | 5 | Alber T|Wozniak J A|Sun D P|Wilson K|Cook S P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":42.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27367,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27368,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3064 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,064 | train | mutant | 374 | 41 | 413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T157F | T157F | 1 | 1 | 0 | 0 | 157 | T | F | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 157 | A | S | false | false | 52.731564 | 18.437143 | 12,626 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:T157F | null | null | null | 4.07 | null | null | null | 4.3 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["SAAFEC_S1262.csv"],"id":45781,"numValue":4.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45782,"numValue":4.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45783,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6948,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3065 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,065 | train | mutant | 1,878 | 41 | 2,106 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D159C | D159C | 1 | 1 | 0 | 0 | 159 | D | C | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 159 | A | G|H | false | false | 79.252348 | 32.745625 | 3,622 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:D159C | 37.1 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":2.4,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13317,"numValue":37.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":13318,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUT... | [{"id":6950,"numValue":3.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3066 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,066 | train | mutant | 1,617 | 41 | 1,818 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A160T | A160T | 1 | 1 | 0 | 0 | 160 | A | T | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 160 | A | G|H | false | false | 26.099318 | 16.993 | 3,032 | ProTherm | 6 | CD | Thermal | Unknown | null | 2LZM_A:A160T | 60 | -5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S1791.csv|Saraboji_S2204.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:A160T","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":11017,"numValue":60.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":11018,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"dataset... | [{"id":6951,"numValue":6.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3067 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,067 | train | mutant | 1,617 | 41 | 1,818 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A160T | A160T | 1 | 1 | 0 | 0 | 160 | A | T | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 160 | A | G|H | false | false | 26.099318 | 16.993 | 6,766 | ProTherm | 6 | CD | Thermal | Unknown | 65.5 | 2LZM_A:A160T | null | null | null | 1.65 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":65.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:A160T","type":"_PD... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24002,"numValue":1.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24003,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6951,"numValue":6.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3069 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,069 | train | mutant | 106 | 41 | 116 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N163D | N163D | 1 | 1 | 0 | 0 | 163 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 163 | A | H | false | false | 121.108788 | 63.36875 | 200 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:N163D | 64.75 | -0.5 | null | null | null | 3.5 | 141 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":827,"numValue":64.75,"references":[],"strValue":null,"type":"TM"},{"datasets":["Saraboji_S1791.csv"],"id":828,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":829,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":830,"numValue":141.0,"... | [{"id":6954,"numValue":7.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3070 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,070 | train | mutant | 106 | 41 | 116 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N163D | N163D | 1 | 1 | 0 | 0 | 163 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 163 | A | H | false | false | 121.108788 | 63.36875 | 212 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:N163D | 61.7 | -0.49 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":877,"numValue":61.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["Saraboji_S1791.csv"],"id":878,"numValue":-0.49,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":879,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":880,"numValue":null,"r... | [{"id":6954,"numValue":7.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3071 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,071 | train | mutant | 106 | 41 | 116 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N163D | N163D | 1 | 1 | 0 | 0 | 163 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 163 | A | H | false | false | 121.108788 | 63.36875 | 6,829 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:N163D | null | null | null | 0.21 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24186,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24187,"numValue":0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24188,"num... | [{"id":6954,"numValue":7.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3072 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,072 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,467 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 57.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64457,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64458,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3073 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,073 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,468 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | null | 80.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64459,"numValue":80.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64460,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3074 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,074 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,469 | ProTherm | 2.3 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | KCl | 0.2 M | 56.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type... | [{"datasets":[],"id":64461,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64462,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:3075 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,075 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,470 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | null | KCl | 0.2 M | 77.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"... | [{"datasets":[],"id":64463,"numValue":77.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64464,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:3076 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,076 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,535 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 71.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 551 | ARTICLE | Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95. | 1,992 | 10.1021/bi00150a028 | 1525170 | Biochemistry;31;8323-8 | 5 | Kuroki R|Matsushima M|Inaka K|Kidokoro S|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64699,"numValue":71.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64700,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3077 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,077 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,120 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 68.8 | null | null | null | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66898,"numValue":68.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66899,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66900,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3078 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,078 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,132 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66935,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66936,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66937,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66938,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3079 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,079 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,133 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66939,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66940,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3081 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,081 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,378 | ProTherm | 3.14 | DSC | Thermal | glycine | 0.05 M | null | 57.8 | null | null | null | 96.4 | null | 97.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.14,"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"}] | [{"datasets":[],"id":67808,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67809,"numValue":96.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67810,"numValue":97.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67811,"numValue":null,"references":[... | |||||||||||||||||||||||||
fireprotdb:3082 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,082 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,379 | ProTherm | 3.04 | DSC | Thermal | glycine | 0.05 M | null | 55.4 | null | null | null | 91.6 | null | 95 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.04,"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"}] | [{"datasets":[],"id":67812,"numValue":55.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67813,"numValue":91.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67814,"numValue":95.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67815,"numValue":null,"references":[... | |||||||||||||||||||||||||
fireprotdb:3083 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,083 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,380 | ProTherm | 2.81 | DSC | Thermal | glycine | 0.05 M | null | 52 | null | null | null | 85.9 | null | 89.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.81,"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"}] | [{"datasets":[],"id":67816,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67817,"numValue":85.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67818,"numValue":89.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67819,"numValue":null,"references":[... | |||||||||||||||||||||||||
fireprotdb:3084 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,084 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,381 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 49.2 | null | null | null | 82.5 | null | 85.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"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"}] | [{"datasets":[],"id":67820,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67821,"numValue":82.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67822,"numValue":85.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67823,"numValue":null,"references":[... | |||||||||||||||||||||||||
fireprotdb:3085 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,085 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,382 | ProTherm | 2.53 | DSC | Thermal | glycine | 0.05 M | null | 45.5 | null | null | null | 75.4 | null | 79.8 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.53,"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"}] | [{"datasets":[],"id":67824,"numValue":45.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67825,"numValue":75.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67826,"numValue":79.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67827,"numValue":null,"references":[... | |||||||||||||||||||||||||
fireprotdb:3086 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,086 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,383 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.1 | 1.58 | 120.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"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"}] | [{"datasets":[],"id":67828,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67829,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67830,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67831,"numValue":120.1,"references":... | |||||||||||||||||||||||||
fireprotdb:3087 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,087 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,402 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"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"}] | [{"datasets":[],"id":67886,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67887,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67888,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3088 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,088 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,121 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"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"}] | [{"datasets":[],"id":70558,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70559,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70560,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":70561,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3089 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,089 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,354 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"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"}] | [{"datasets":[],"id":71276,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71277,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71278,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":71279,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3090 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,090 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,388 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.01 | 1.58 | 119.98 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"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"}] | [{"datasets":[],"id":71373,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71374,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71375,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":71376,"numValue":119.98,"references... | |||||||||||||||||||||||||
fireprotdb:3091 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,091 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,691 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 64.9 | null | null | null | 114.1 | 1.58 | 120.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"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"}] | [{"datasets":[],"id":72420,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72421,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72422,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72423,"numValue":120.1,"references":... | |||||||||||||||||||||||||
fireprotdb:3092 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,092 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,697 | ProTherm | 2.63 | DSC | Thermal | glycine-HCl | 50 mM | null | 55.6 | null | null | null | 90.58 | 1.94 | 96.32 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.63,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72438,"numValue":55.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72439,"numValue":90.58,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72440,"numValue":1.94,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72441,"numValue":96.32,"references":... | |||||||||||||||||||||||||
fireprotdb:3093 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,093 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,698 | ProTherm | 2.64 | DSC | Thermal | glycine-HCl | 50 mM | null | 56.4 | null | null | null | 95.12 | 1.63 | 95.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.64,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72443,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72444,"numValue":95.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72445,"numValue":1.63,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72446,"numValue":95.6,"references":[... | |||||||||||||||||||||||||
fireprotdb:3094 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,094 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,699 | ProTherm | 2.68 | DSC | Thermal | glycine-HCl | 50 mM | null | 56.8 | null | null | null | 92.02 | 1.94 | 96.32 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.68,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72448,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72449,"numValue":92.02,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72450,"numValue":1.94,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72451,"numValue":96.32,"references":... | |||||||||||||||||||||||||
fireprotdb:3095 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,095 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,700 | ProTherm | 2.75 | DSC | Thermal | glycine-HCl | 50 mM | null | 58.2 | null | null | null | 97.51 | 1.77 | 98.95 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.75,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72453,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72454,"numValue":97.51,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72455,"numValue":1.77,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72456,"numValue":98.95,"references":... | |||||||||||||||||||||||||
fireprotdb:3096 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,096 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,701 | ProTherm | 2.78 | DSC | Thermal | glycine-HCl | 50 mM | null | 59 | null | null | null | 97.99 | 1.31 | 101.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72458,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72459,"numValue":97.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72460,"numValue":1.31,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72461,"numValue":101.1,"references":... | |||||||||||||||||||||||||
fireprotdb:3097 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,097 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,702 | ProTherm | 2.84 | DSC | Thermal | glycine-HCl | 50 mM | null | 60.3 | null | null | null | 98.47 | 1.67 | 103.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72463,"numValue":60.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72464,"numValue":98.47,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72465,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72466,"numValue":103.01,"references"... | |||||||||||||||||||||||||
fireprotdb:3098 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,098 | train | sequence | 48 | 48 | -1 | 148 | -1 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,703 | ProTherm | 2.87 | DSC | Thermal | glycine-HCl | 50 mM | null | 60.5 | null | null | null | 98.95 | 1.7 | 98.95 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1277 | ARTICLE | Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. | 2,000 | 10.1093/protein/13.4.299 | 10810162 | Protein Eng;13;299-307 | 5 | Takano K|Yamagata Y|Yutani K|Katakura Y|Goda S | [{"numValue":2.87,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72468,"numValue":60.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72469,"numValue":98.95,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72470,"numValue":1.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":72471,"numValue":98.95,"references":[... |
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