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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:1332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,332 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,914 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 65.3 | null | null | null | null | 2.5 | 130 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":66228,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66229,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66230,"numValue":130.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66231,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,333 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,915 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 65.3 | null | null | null | null | 2.5 | 132 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":66232,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66233,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66234,"numValue":132.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66235,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,334 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,941 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 51.65 | null | null | null | null | null | 114 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":66350,"numValue":51.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66351,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66352,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,335 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,974 | ProTherm | 2.1 | CD | Thermal | H3PO4 | 17 mM | null | KCl | 0.15 M | 42 | null | null | null | null | null | 87 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":2.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValu... | [{"datasets":[],"id":66466,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66467,"numValue":87.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66468,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,336 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,975 | ProTherm | 5.8 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 0.15 M | 66.3 | null | null | null | null | null | 144 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 40 | ARTICLE | Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties. | 1,993 | 10.1002/prot.340150407 | 8460110 | Proteins;15;401-12 | 4 | Matthews B W|Wozniak J A|Pjura P|McIntosh L P | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":66469,"numValue":66.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66470,"numValue":144.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66471,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1337 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,337 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,976 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 M,17 M, | null | KCl | 25 mM | 51.7 | null | null | null | null | null | 117 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 43 | ARTICLE | Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe. | 1,993 | 10.1002/pro.5560020811 | 8401213 | Protein Sci;2;1285-90 | 5 | Nicholson H|Baase W A|Matthews B W|Anderson D E|Hurley J H | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 M,17 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION... | [{"datasets":[],"id":66472,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66473,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66474,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,338 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,977 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 65.09 | null | null | null | null | null | 134 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 43 | ARTICLE | Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe. | 1,993 | 10.1002/pro.5560020811 | 8401213 | Protein Sci;2;1285-90 | 5 | Nicholson H|Baase W A|Matthews B W|Anderson D E|Hurley J H | [{"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":66475,"numValue":65.09,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66476,"numValue":134.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66477,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,339 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,978 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 51.55 | null | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"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":66478,"numValue":51.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66479,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66480,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,340 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,989 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66512,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66513,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,341 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,997 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 150 mM | 38.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":2.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":66542,"numValue":38.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66543,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,342 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,998 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 63.2 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66544,"numValue":63.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66545,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,343 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,999 | ProTherm | 3.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 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|ION|ION_CONC | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":3.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66546,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66547,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1344 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,344 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,000 | ProTherm | 4 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 62.2 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":4.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66548,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66549,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,345 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,001 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 65.7 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66550,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66551,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,346 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,006 | ProTherm | 3 | CD | Thermal | Unknown | null | NaCl | 0.2 M | 56.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 51 | ARTICLE | Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. | 1,984 | 10.1016/0022-2836(84)90474-1 | 6726809 | J Mol Biol;175;195-212 | 3 | Hawkes R|Schellman J|Grutter M G | [{"numValue":3.0,"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":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"}] | [{"datasets":[],"id":66566,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66567,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1347 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,347 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,012 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 51.76 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":66585,"numValue":51.76,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66586,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,348 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,013 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 64.89 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":[],"id":66587,"numValue":64.89,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66588,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,349 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,017 | ProTherm | 2.2 | CD | Thermal | Sodium phosphate | 0.2 M | null | NaCl | 0.5 M | 42.6 | null | null | null | null | null | 107 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 59 | ARTICLE | Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. | 1,977 | 10.1016/0005-2795(77)90166-0 | 911878 | Biochim Biophys Acta;494;367-83 | 2 | Schellman J A|Elwell M L | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":66601,"numValue":42.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66602,"numValue":107.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66603,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,350 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,018 | ProTherm | 2.5 | CD | Thermal | Sodium phosphate | 0.2 M | null | NaCl | 0.5 M | 46.2 | null | null | null | null | null | 122 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 59 | ARTICLE | Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. | 1,977 | 10.1016/0005-2795(77)90166-0 | 911878 | Biochim Biophys Acta;494;367-83 | 2 | Schellman J A|Elwell M L | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":66604,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66605,"numValue":122.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66606,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,351 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,019 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 41.9 | null | null | null | null | 2 | 89 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":66607,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66608,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66609,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66610,"numValue":null,"references":[... | |||||||||||||||||||||||
fireprotdb:1352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,352 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,020 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 64.7 | null | null | null | null | 2 | 129 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":66611,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66612,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66613,"numValue":129.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66614,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1353 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,353 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,042 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 40.75 | null | null | null | null | 2.4 | 86 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"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"}] | [{"datasets":[],"id":66695,"numValue":40.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66696,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66697,"numValue":86.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66698,"numValue":null,"references":... | ||||||||||||||||||||||||
fireprotdb:1354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,354 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,045 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 51.6 | null | null | null | null | 1.8 | 117 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":3.0,"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":66704,"numValue":51.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66705,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66706,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66707,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,355 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,046 | ProTherm | 4.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 64.6 | null | null | null | null | 1.8 | 138 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":4.4,"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":[],"id":66708,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66709,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66710,"numValue":138.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66711,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1356 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,356 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,047 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 65.3 | null | null | null | null | 1.8 | 135 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":5.3,"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":66712,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66713,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66714,"numValue":135.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66715,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,357 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,048 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 61.9 | null | null | null | null | 1.8 | 121 | null | null | null | null | null | null | null | null | null | yes(50-75%) | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":6.5,"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":66716,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66717,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66718,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66719,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1358 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,358 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,049 | ProTherm | 10.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 47.9 | null | null | null | null | 1.8 | 79.5 | null | null | null | null | null | null | null | null | null | yes(20%) | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 65 | ARTICLE | Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. | 1,991 | 10.1021/bi00113a006 | 1747370 | Biochemistry;30;11521-9 | 5 | Baase W A|Matthews B W|Dao-pin S|Anderson D E|Dahlquist F W | [{"numValue":10.4,"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":"... | [{"datasets":[],"id":66720,"numValue":47.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66721,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66722,"numValue":79.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66723,"numValue":null,"references":[... | |||||||||||||||||||||||
fireprotdb:1359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,359 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,051 | ProTherm | 5.31 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 65.3 | 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 | 67 | ARTICLE | Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. | 1,991 | 10.1021/bi00219a037 | 1991123 | Biochemistry;30;1425-32 | 4 | Nicholson H|Matthews B W|Poteete A R|Sun D P | [{"numValue":5.31,"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":"... | [{"datasets":[],"id":66727,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66728,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,360 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,052 | ProTherm | 3 | CD | Thermal | HCl | null | 51.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 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"}] | [{"datasets":[],"id":66729,"numValue":51.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66730,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:1362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,362 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,054 | ProTherm | 4 | CD | Thermal | Sodium acetate | 20 mM | null | KCl | 0.2 M | 62.8 | 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 | 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":66733,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66734,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,363 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,055 | ProTherm | 6 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 64.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":66735,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66736,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,364 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,060 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 41.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":66751,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66752,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,365 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,061 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 64.7 | 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 | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":66753,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66754,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,366 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,062 | ProTherm | 1.99 | CD | Thermal | Unknown | null | KCl | 0.2 M | 41.4 | null | null | null | null | null | 87 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":1.99,"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"}] | [{"datasets":[],"id":66755,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66756,"numValue":87.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66757,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,367 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,063 | ProTherm | 2.86 | CD | Thermal | Unknown | null | KCl | 0.2 M | 52.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 79 | ARTICLE | Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants. | 1,989 | 10.1073/pnas.86.21.8237 | 2682639 | Proc Natl Acad Sci U S A;86;8237-41 | 4 | Baase W A|Matthews B W|Matsumura M|Karpusas M | [{"numValue":2.86,"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"}] | [{"datasets":[],"id":66758,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66759,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,368 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,077 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 41.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"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"}] | [{"datasets":[],"id":66790,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66791,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,369 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,078 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 64.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"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"}] | [{"datasets":[],"id":66792,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66793,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,370 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,084 | ProTherm | 2 | CD | Thermal | H3PO4,HCl, | 10 mM,10 mM, | null | KCl | 0.2 M | 41.9 | null | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,HCl,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION... | [{"datasets":[],"id":66805,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66806,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66807,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,371 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,085 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 64.7 | null | null | null | null | null | 129 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":6.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66808,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66809,"numValue":129.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66810,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,372 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,087 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 65 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"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"}] | [{"datasets":[],"id":66813,"numValue":65.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66814,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,373 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,088 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 39.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":66815,"numValue":39.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66816,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,374 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,089 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 62.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":66817,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66818,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1375 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,375 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,090 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 41.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 90 | ARTICLE | Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. | 1,987 | 10.2210/pdb1l16/pdb | 3680274 | J Biol Chem;262;16858-64 | 2 | Matthews B W|Gray T M | [{"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"}] | [{"datasets":[],"id":66819,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66820,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,377 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,092 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 42 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"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"}] | [{"datasets":[],"id":66823,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66824,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1378 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,378 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,093 | ProTherm | 4 | CD | Thermal | Unknown | null | KCl | 0.2 M | 63 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"numValue":4.0,"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"}] | [{"datasets":[],"id":66825,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66826,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,379 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,094 | ProTherm | 6 | CD | Thermal | Unknown | null | KCl | 0.2 M | 66 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 91 | ARTICLE | Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. | 1,988 | 10.1126/science.3277275 | 3277275 | Science;239;631-5 | 5 | Alber T|Nicholson H|Wozniak J A|Sun D P|Bell J A | [{"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":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"}] | [{"datasets":[],"id":66827,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66828,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,380 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,095 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 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 | 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":66829,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66830,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1381 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,381 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,096 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 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 | 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":66831,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66832,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,382 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,097 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 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 | 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":66833,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66834,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1383 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,383 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,098 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 38.75 | 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 | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"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":66835,"numValue":38.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66836,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,384 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,099 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 46.16 | 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 | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"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":66837,"numValue":46.16,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66838,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,385 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,100 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 53.56 | 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 | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"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":66839,"numValue":53.56,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66840,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1386 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,386 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,101 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 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 | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|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":66841,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66842,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,387 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,102 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 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 | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|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":66843,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66844,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1388 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,388 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,103 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 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 | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|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":66845,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66846,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,389 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,104 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 53.42 | null | null | null | null | 1.8 | 127 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66847,"numValue":53.42,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66848,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66849,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66850,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:1390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,390 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,105 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 66.51 | null | null | null | null | 2.5 | 140 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":66851,"numValue":66.51,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66852,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66853,"numValue":140.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66854,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:1392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,392 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,107 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 65.1 | null | null | null | null | 3.5 | 131 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":66859,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66860,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66861,"numValue":131.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66862,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,393 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,108 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 51.68 | null | null | null | null | null | 114 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":66863,"numValue":51.68,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66864,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66865,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1395 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,395 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,110 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 51.76 | null | null | null | null | null | 119 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":66869,"numValue":51.76,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66870,"numValue":119.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66871,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1396 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,396 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,111 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 64.88 | null | null | null | null | null | 133 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":66872,"numValue":64.88,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66873,"numValue":133.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66874,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1397 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,397 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,112 | ProTherm | 2 | CD | Thermal | KCl-HCl | null | KCl | 15 mM | 41 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KCl-HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"15 mM","type":"ION_CONC"}] | [{"datasets":[],"id":66875,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66876,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1398 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,398 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,113 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 15 mM | 63 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":66877,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66878,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,399 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,114 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 54.1 | null | null | null | null | null | 130.8 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"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":66879,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66880,"numValue":130.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66881,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,401 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,116 | ProTherm | 2.83 | CD | Thermal | Unknown | null | KCl | 0.2 M | 51.1 | null | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"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"}] | [{"datasets":[],"id":66885,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66886,"numValue":108.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66887,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,402 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,189 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 65.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 125 | ARTICLE | Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. | 1,993 | 10.1002/pro.5560021222 | 8298466 | Protein Sci;2;2226-32 | 2 | Matthews B W|Pjura P | [{"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":67133,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67134,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,403 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,237 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 65.3 | null | null | null | null | null | 130 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":[],"id":67294,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67295,"numValue":130.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67296,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":67297,"numValue":null,"references... | ||||||||||||||||||||||
fireprotdb:1404 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,404 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,302 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 41.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67532,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67533,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:1405 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,405 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,357 | ProTherm | 6.8 | Fluorescence | Thermal | cacodylate | 50 mM | null | NaCl | 0.2 M | 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 | 906 | ARTICLE | Effect of an engineered disulfide bond on the folding of T4 lysozyme at low temperatures. | 1,990 | 10.1021/bi00465a026 | 2334694 | Biochemistry;29;3331-7 | 4 | Wetzel R|Perry L J|Fink A L|Anderson W D | [{"numValue":6.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":67748,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67749,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1406 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,406 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,374 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 51.7 | null | null | null | null | 1.8 | 113 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":67795,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67796,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67797,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67798,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:1407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,407 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,384 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 40.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":67833,"numValue":40.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67834,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1409 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,409 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,425 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 40.4 | null | null | null | null | null | 99 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":67961,"numValue":40.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67962,"numValue":99.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67963,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,410 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,426 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 52.6 | null | null | null | null | null | 123 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":67964,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67965,"numValue":123.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67966,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1411 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,411 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,427 | ProTherm | 4 | CD | Thermal | acetate | 10 mM | null | KCl | 0.15 M | 63.6 | null | null | null | null | null | 143 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":67967,"numValue":63.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67968,"numValue":143.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67969,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1412 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,412 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,428 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | null | KCl | 0.15 M | 66.7 | null | null | null | null | null | 142 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":67970,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67971,"numValue":142.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67972,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1413 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,413 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,429 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 64.6 | null | null | null | null | null | 125 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":67973,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67974,"numValue":125.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67975,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,414 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,447 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 66 | 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 | 303 | ARTICLE | pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. | 1,990 | 10.1021/bi00461a025 | 2337607 | Biochemistry;29;2403-8 | 3 | Anderson D E|Becktel W J|Dahlquist F W | [{"numValue":5.5,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":68028,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68029,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,415 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,518 | ProTherm | 1.8 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 35.6 | null | null | null | 86.7 | 2.67 | 87.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":1.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":68305,"numValue":35.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68306,"numValue":86.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68307,"numValue":2.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68308,"numValue":87.6,"references":[]... | |||||||||||||||||||||||
fireprotdb:1416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,416 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,519 | ProTherm | 2 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 38.75 | null | null | null | 97 | 2.4 | 89.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":68310,"numValue":38.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68311,"numValue":97.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68312,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68313,"numValue":89.1,"references":[]... | |||||||||||||||||||||||
fireprotdb:1418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,418 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,521 | ProTherm | 2.34 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 42.94 | null | null | null | 111.3 | 2.53 | 93.5 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.34,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":68320,"numValue":42.94,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68321,"numValue":111.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68322,"numValue":2.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68323,"numValue":93.5,"references":... | |||||||||||||||||||||||
fireprotdb:1419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,419 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,522 | ProTherm | 2.4 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 43.7 | null | null | null | 114.2 | 2.49 | 99.7 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":68325,"numValue":43.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68326,"numValue":114.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68327,"numValue":2.49,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68328,"numValue":99.7,"references":[... | |||||||||||||||||||||||
fireprotdb:1420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,420 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,523 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 45.03 | null | null | null | 114.6 | 2.16 | 95.8 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":68330,"numValue":45.03,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68331,"numValue":114.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68332,"numValue":2.16,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68333,"numValue":95.8,"references":... | |||||||||||||||||||||||
fireprotdb:1421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,421 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,524 | ProTherm | 2.7 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 48.7 | null | null | null | 114.6 | 2.33 | 102.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":68335,"numValue":48.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68336,"numValue":114.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68337,"numValue":2.33,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68338,"numValue":102.4,"references":... | |||||||||||||||||||||||
fireprotdb:1422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,422 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,525 | ProTherm | 2.84 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 51.68 | null | null | null | 123.6 | 2.5 | 106.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 14 | ARTICLE | A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96----His mutant form thereof. | 1,989 | 10.1021/bi00435a024 | 2665807 | Biochemistry;28;3788-92 | 2 | Kitamura S|Sturtevant J M | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":68340,"numValue":51.68,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68341,"numValue":123.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68342,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":68343,"numValue":106.9,"references":... | |||||||||||||||||||||||
fireprotdb:1423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,423 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,711 | ProTherm | 2 | CD | Thermal | HCl | null | KCl | 0.20 M | 40.8 | null | null | null | null | null | 86 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.0,"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":"KCl","type":"ION"},{"numValue":null,"strValue":"0.20 M","type":"ION_CONC"}] | [{"datasets":[],"id":68979,"numValue":40.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68980,"numValue":86.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":68981,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:1424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,424 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,805 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 45 | null | null | null | 113.6 | null | null | null | null | null | null | null | null | null | null | null | yes (>90%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1160 | ARTICLE | Circular permutation of T4 lysozyme. | 1,993 | 10.1021/bi00097a006 | 8241117 | Biochemistry;32;12311-8 | 4 | Alber T|Zhang T|Bertelsen E|Benvegnu D | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":69329,"numValue":45.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69330,"numValue":113.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69331,"numValue":null,"references":[],"strValue":"yes (>90%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,425 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,806 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 44 | null | null | null | 84 | null | null | null | null | null | null | null | null | null | null | null | yes (>90%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1160 | ARTICLE | Circular permutation of T4 lysozyme. | 1,993 | 10.1021/bi00097a006 | 8241117 | Biochemistry;32;12311-8 | 4 | Alber T|Zhang T|Bertelsen E|Benvegnu D | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":69332,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69333,"numValue":84.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69334,"numValue":null,"references":[],"strValue":"yes (>90%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,426 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,807 | ProTherm | 2.5 | DSC | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 40.1 | null | null | null | 68 | null | null | null | null | null | null | null | null | null | null | null | yes (>90%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1160 | ARTICLE | Circular permutation of T4 lysozyme. | 1,993 | 10.1021/bi00097a006 | 8241117 | Biochemistry;32;12311-8 | 4 | Alber T|Zhang T|Bertelsen E|Benvegnu D | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":69335,"numValue":40.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69336,"numValue":68.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69337,"numValue":null,"references":[],"strValue":"yes (>90%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,427 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,854 | ProTherm | 2.5 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 47.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 325 | ARTICLE | Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices. | 1,994 | 10.1021/bi00206a003 | 7918421 | Biochemistry;33;12022-31 | 5 | Cornish V W|Kaplan M I|Veenstra D L|Kollman P A|Schultz P G | [{"numValue":2.5,"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":69546,"numValue":47.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69547,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,428 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,982 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 36.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":70030,"numValue":36.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70031,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,429 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,212 | ProTherm | 5.42 | DSC | Thermal | Sodium acetate,Acetic acid, | 8.6 mM,1.4 mM, | null | NaCl | 0.10 M | 65.3 | 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 | 913 | ARTICLE | Substitution with selenomethionine can enhance the stability of methionine-rich proteins. | 1,999 | 10.1006/jmbi.1999.3220 | 10556025 | J Mol Biol;294;17-20 | 4 | Baase W A|Matthews B W|Gassner N C|Hausrath A C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"8.6 mM,1.4 mM,","type":"BUFFER_CONC"},{"numValue":null,"strVal... | [{"datasets":[],"id":70853,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70854,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,430 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,318 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 51.7 | null | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|Baase W A|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":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":[],"id":71195,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71196,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71197,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,431 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,347 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 51.7 | null | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":3.0,"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":71257,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71258,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71259,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,432 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,348 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 65.2 | null | null | null | null | null | 128 | null | null | null | null | null | null | null | null | null | yes(>80%) | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"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":71260,"numValue":65.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71261,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":71262,"numValue":null,"references":[],"strValue":"yes(>80%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,433 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,500 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 65 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 374 | ARTICLE | Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. | 1,996 | 10.1002/pro.5560050419 | 8845764 | Protein Sci;5;742-51 | 5 | Blankespoor S|Born T|Jagar R|Gray T M|Arnoys E J | [{"numValue":7.0,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":71791,"numValue":65.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71792,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:1435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,435 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,507 | ProTherm | 2.6 | DSC | Thermal | glycine-HCl | 20 mM | null | 45.6 | null | null | null | 111.85 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":2.6,"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":"20 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71808,"numValue":45.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71809,"numValue":111.85,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71810,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:1436 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,436 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,508 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 20 mM | null | 49.8 | null | null | null | 120.22 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"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":"20 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71811,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71812,"numValue":120.22,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71813,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:1437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,437 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,509 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 20 mM | null | 54.1 | null | null | null | 127.39 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"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":"20 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71814,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71815,"numValue":127.39,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71816,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:1438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,438 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,510 | ProTherm | 3.3 | DSC | Thermal | glycine-HCl | 20 mM | null | 59.4 | null | null | null | 134.08 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.3,"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":"20 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71817,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71818,"numValue":134.08,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71819,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:1439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,439 | train | sequence | 41 | 41 | -1 | 164 | -1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,511 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 20 mM | null | 62.1 | null | null | null | 136.47 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.5,"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":"20 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":71820,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71821,"numValue":136.47,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":71822,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] |
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