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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:14065 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,065 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,904 | ProTherm | 10 | DSC | Thermal | CAPS | 50 mM | null | 48.6 | null | null | null | 122 | null | null | null | null | null | null | null | null | null | null | null | yes (~80%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 912 | ARTICLE | A calorimetric study of the thermal stability of barstar and its interaction with barnase. | 1,995 | 10.1021/bi00015a036 | 7711042 | Biochemistry;34;5224-33 | 5 | Schreiber G|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":10.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"CAPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69753,"numValue":48.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69754,"numValue":122.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69755,"numValue":null,"references":[],"strValue":"yes (~80%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14066 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,066 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,905 | ProTherm | 10.3 | DSC | Thermal | CAPS | 50 mM | null | 48.4 | null | null | null | 121.3 | null | null | null | null | null | null | null | null | null | null | null | yes (~80%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 912 | ARTICLE | A calorimetric study of the thermal stability of barstar and its interaction with barnase. | 1,995 | 10.1021/bi00015a036 | 7711042 | Biochemistry;34;5224-33 | 5 | Schreiber G|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":10.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"CAPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69756,"numValue":48.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69757,"numValue":121.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69758,"numValue":null,"references":[],"strValue":"yes (~80%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14067 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,067 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,906 | ProTherm | 10.5 | DSC | Thermal | CAPS | 50 mM | null | 47.4 | null | null | null | 119.6 | null | null | null | null | null | null | null | null | null | null | null | yes (~80%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 912 | ARTICLE | A calorimetric study of the thermal stability of barstar and its interaction with barnase. | 1,995 | 10.1021/bi00015a036 | 7711042 | Biochemistry;34;5224-33 | 5 | Schreiber G|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":10.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"CAPS","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69759,"numValue":47.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69760,"numValue":119.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69761,"numValue":null,"references":[],"strValue":"yes (~80%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14068 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,068 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,211 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | null | 54.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":70851,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70852,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14069 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,069 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,617 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | null | 51.5 | null | null | null | 126.67 | null | 126.48 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1266 | ARTICLE | Insertion in barnase of a loop sequence from ribonuclease T1. Investigating sequence and structure alignments by protein engineering. | 1,994 | 10.1111/j.1432-1033.1994.tb18817.x | 8181455 | Eur J Biochem;221;1003-12 | 2 | Vuilleumier S|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72193,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72194,"numValue":126.67,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":72195,"numValue":126.48,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":72196,"numValue":null,"reference... | |||||||||||||||||||||||||
fireprotdb:14070 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,070 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,525 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | null | null | 8.69 | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":74995,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":74996,"numValue":8.69,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74997,"numValue":null,"references":[],"strValue":"yes (>95%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14071 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,071 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,526 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | null | null | 8.66 | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":74998,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":74999,"numValue":8.66,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75000,"numValue":null,"references":[],"strValue":"yes (>95%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14073 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,073 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,600 | ProTherm | 6.3 | Fluorescence | GdnHCl | MES | 450 mM | 25 | null | null | 8.88 | null | null | null | null | 1.97 | 4.51 | null | null | null | null | null | null | null | yes (100%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFF... | [{"datasets":[],"id":75251,"numValue":8.88,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75252,"numValue":4.51,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75253,"numValue":1.97,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75254,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14074 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,074 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,643 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | null | null | 8.8 | null | null | null | null | 4.57 | 1.93 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":75391,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75392,"numValue":1.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75393,"numValue":4.57,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75394,"numValue":null,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:14075 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,075 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,644 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | null | null | 8.83 | null | null | null | null | 4.6 | 1.92 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|Fersht A R|Matthews J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFFER... | [{"datasets":[],"id":75395,"numValue":8.83,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75396,"numValue":1.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75397,"numValue":4.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75398,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:14076 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,076 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,659 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | null | null | 10.5 | null | null | null | null | 2.27 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 645 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 1,988 | 10.1038/333784a0 | 3386721 | Nature;333;784-6 | 4 | Nyberg K|Fersht A R|Kellis J T|Sali D | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":[],"id":75442,"numValue":10.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75443,"numValue":2.27,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75444,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14077 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,077 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,662 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | null | null | 8.82 | null | null | null | null | 4.57 | 1.93 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":75453,"numValue":8.82,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75454,"numValue":1.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75455,"numValue":4.57,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75456,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14078 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,078 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,666 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | null | null | 8.82 | null | null | null | null | 4.58 | 1.92 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":75469,"numValue":8.82,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75470,"numValue":1.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75471,"numValue":4.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75472,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14079 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,079 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,668 | ProTherm | 5.8 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | null | null | 11 | null | null | null | null | 5.62 | 1.95 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":75475,"numValue":11.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75476,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75477,"numValue":5.62,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75478,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:14080 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,080 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,669 | ProTherm | 9 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | null | null | 9.41 | null | null | null | null | 4.8 | 2.11 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":75479,"numValue":9.41,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75480,"numValue":2.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75481,"numValue":4.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75482,"numValue":null,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:14081 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,081 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,701 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | null | null | 10.15 | null | null | null | null | 4.57 | 2.22 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 671 | ARTICLE | Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. | 1,991 | 10.1016/0022-2836(91)90725-l | 2010920 | J Mol Biol;218;465-75 | 3 | Serrano L|Bycroft M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":75603,"numValue":10.15,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75604,"numValue":2.22,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75605,"numValue":4.57,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75606,"numValue":null,"references":[],... | |||||||||||||||||||||||
fireprotdb:14082 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,082 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,742 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 50 mM | 25 | null | null | 10.01 | null | null | null | null | 4.53 | 2.21 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 700 | ARTICLE | Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. | 1,990 | 10.1021/bi00492a006 | 2248951 | Biochemistry;29;9343-52 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":75751,"numValue":10.01,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75752,"numValue":2.21,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75753,"numValue":4.53,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75754,"numValue":null,"references":[],... | |||||||||||||||||||||||||
fireprotdb:14084 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,084 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,796 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | null | null | 8.83 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 706 | ARTICLE | Effect of active site residues in barnase on activity and stability. | 1,992 | 10.1016/0022-2836(92)90387-y | 1602471 | J Mol Biol;225;585-9 | 3 | Serrano L|Fersht A R|Meiering E M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":75915,"numValue":8.83,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75916,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14085 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,085 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,800 | ProTherm | 4.4 | NMR | Urea | Sodium acetate | 30 mM | 25 | NaCl | 1 M | null | null | 8.13 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFE... | [{"datasets":[],"id":75927,"numValue":8.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75928,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14086 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,086 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,801 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | null | null | 8.05 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":8.9,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":75929,"numValue":8.05,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75930,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14088 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,088 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,808 | ProTherm | 3 | DSC | Thermal | Potassium acetate | 50 mM | 25 | null | null | 4.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":75947,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75948,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14089 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,089 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,809 | ProTherm | 3.5 | DSC | Thermal | Potassium acetate | 50 mM | 25 | null | null | 6.79 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":75949,"numValue":6.79,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75950,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14090 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,090 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,810 | ProTherm | 4 | DSC | Thermal | Potassium acetate | 50 mM | 25 | null | null | 8.13 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":75951,"numValue":8.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75952,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14091 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,091 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,811 | ProTherm | 4.5 | DSC | Thermal | Potassium acetate | 50 mM | 25 | null | null | 9.02 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":75953,"numValue":9.02,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75954,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14092 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,092 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,812 | ProTherm | 5 | DSC | Thermal | Potassium acetate | 50 mM | 25 | null | null | 9.35 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1142 | ARTICLE | A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. | 1,994 | 10.1021/bi00179a018 | 8142395 | Biochemistry;33;3919-26 | 5 | el Harrous M|Fersht A R|Mart?nez J C|Filimonov V V|Mateo P L | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":75955,"numValue":9.35,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75956,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14093 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,093 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,831 | ProTherm | 6 | CD | Thermal | MES | 50 mM | 25 | null | null | 10 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1395 | ARTICLE | Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. | 1,994 | 10.1021/bi00195a026 | 8038174 | Biochemistry;33;8826-32 | 3 | Vuilleumier S|Oliveberg M|Fersht A R | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":76039,"numValue":10.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76040,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14094 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,094 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,833 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | null | null | 8.79 | null | null | null | null | 4.58 | 1.92 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 926 | ARTICLE | Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. | 1,993 | 10.1021/bi00067a022 | 8476861 | Biochemistry;32;4322-9 | 2 | Clarke J|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFFER... | [{"datasets":[],"id":76044,"numValue":8.79,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76045,"numValue":1.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76046,"numValue":4.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76047,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14095 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,095 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,834 | ProTherm | 6.3 | Fluorescence | GdnHCl | MES | 450 mM | 25 | null | null | 8.8 | null | null | null | null | 2 | 4.4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 926 | ARTICLE | Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. | 1,993 | 10.1021/bi00067a022 | 8476861 | Biochemistry;32;4322-9 | 2 | Clarke J|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFF... | [{"datasets":[],"id":76048,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76049,"numValue":4.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76050,"numValue":2.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76051,"numValue":null,"references":[],"str... | |||||||||||||||||||||||||
fireprotdb:14096 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,096 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,850 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | NaCl | 0.15 M | null | null | 8.79 | null | null | null | null | 4.58 | 1.92 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 713 | ARTICLE | Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. | 1,993 | 10.1021/bi00212a026 | 8257694 | Biochemistry;32;13584-92 | 2 | Fersht A R|Sanz J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":76101,"numValue":8.79,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76102,"numValue":1.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76103,"numValue":4.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76104,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:14097 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,097 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,856 | ProTherm | 6.3 | CD | Urea | MES | 50 mM | 25 | null | null | 9.18 | null | null | null | null | 4.53 | 2.02 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1405 | ARTICLE | Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains. | 1,993 | 10.1021/bi00090a005 | 8399173 | Biochemistry;32;10303-13 | 4 | Vuilleumier S|Sancho J|Loewenthal R|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":76128,"numValue":9.18,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76129,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76130,"numValue":4.53,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76131,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14098 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,098 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,857 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | null | null | 8.79 | null | null | null | null | 4.58 | 1.92 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1405 | ARTICLE | Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains. | 1,993 | 10.1021/bi00090a005 | 8399173 | Biochemistry;32;10303-13 | 4 | Vuilleumier S|Sancho J|Loewenthal R|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":76132,"numValue":8.79,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76133,"numValue":1.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76134,"numValue":4.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76135,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14099 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,099 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,885 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 25 | KCl | null | null | 10.2 | null | null | 1.88 | 84.5 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION | 1416 | ARTICLE | Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH. | 1,996 | 10.1021/bi950967t | 8611580 | Biochemistry;35;2738-49 | 2 | Oliveberg M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":76242,"numValue":1.88,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":76243,"numValue":84.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":76244,"numValue":10.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76245,"numValue":null,"references":... | ||||||||||||||||||||||||
fireprotdb:14100 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,100 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,889 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 25 | null | null | 10.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 718 | ARTICLE | pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds. | 1,995 | 10.1021/bi00029a018 | 7626612 | Biochemistry;34;9424-33 | 3 | Oliveberg M|Fersht A R|Arcus V L | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":76254,"numValue":10.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76255,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14101 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,101 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,892 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1 M | 25 | null | null | 8.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 719 | ARTICLE | Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase. | 1,995 | 10.1021/bi00020a027 | 7756312 | Biochemistry;34;6805-14 | 2 | Fersht A R|Matthews J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1 M","type":"BUFFER_CO... | [{"datasets":[],"id":76261,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76262,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14103 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,103 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,260 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | null | null | null | null | null | null | null | 4.58 | null | null | null | null | null | null | null | null | yes | CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":77362,"numValue":4.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77363,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14105 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,105 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,268 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | 25 | null | null | 8.52 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1266 | ARTICLE | Insertion in barnase of a loop sequence from ribonuclease T1. Investigating sequence and structure alignments by protein engineering. | 1,994 | 10.1111/j.1432-1033.1994.tb18817.x | 8181455 | Eur J Biochem;221;1003-12 | 2 | Vuilleumier S|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":77388,"numValue":8.52,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77389,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14106 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,106 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,313 | ProTherm | 6.3 | CD | GdnSCN | Sodium acetate | 50 mM | 25 | null | null | 11 | null | null | null | null | 0.77 | 14.31 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1461 | ARTICLE | Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module. | 2,000 | 10.1110/ps.9.1.112 | 10739253 | Protein Sci;9;112-20 | 2 | Cota E|Clarke J | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnSCN","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":77536,"numValue":11.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77537,"numValue":14.31,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77538,"numValue":0.77,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77539,"numValue":null,"references":[],... | |||||||||||||||||||||||||
fireprotdb:14107 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,107 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,370 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | null | null | 9.93 | null | null | null | null | 4.58 | 2.02 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":77732,"numValue":9.93,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77733,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77734,"numValue":4.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":77735,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14109 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,109 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,701 | ProTherm | 2.87 | Fluorescence | Urea | diglycine | 30 mM | 20 | null | null | 3.63 | null | null | null | null | 1.14 | 3.19 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1389 | ARTICLE | Urea denaturation of barnase: pH dependence and characterization of the unfolded state. | 1,992 | 10.1021/bi00125a013 | 1547213 | Biochemistry;31;2728-34 | 3 | Pace C N|Erickson R E|Laurents D V | [{"numValue":2.87,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"diglycine","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"... | [{"datasets":[],"id":78742,"numValue":3.63,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78743,"numValue":3.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78744,"numValue":1.14,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78745,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14110 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,110 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,702 | ProTherm | 2.82 | Fluorescence | Urea | diglycine | 30 mM | 20 | NaCl | 0.1 M | null | null | 3.58 | null | null | null | null | 1.21 | 2.97 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1389 | ARTICLE | Urea denaturation of barnase: pH dependence and characterization of the unfolded state. | 1,992 | 10.1021/bi00125a013 | 1547213 | Biochemistry;31;2728-34 | 3 | Pace C N|Erickson R E|Laurents D V | [{"numValue":2.82,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"diglycine","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"... | [{"datasets":[],"id":78746,"numValue":3.58,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78747,"numValue":2.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78748,"numValue":1.21,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78749,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:14111 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,111 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,703 | ProTherm | 2.76 | Fluorescence | Urea | diglycine | 30 mM | 20 | NaCl | 0.5 M | null | null | 4.2 | null | null | null | null | 1.61 | 2.62 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1389 | ARTICLE | Urea denaturation of barnase: pH dependence and characterization of the unfolded state. | 1,992 | 10.1021/bi00125a013 | 1547213 | Biochemistry;31;2728-34 | 3 | Pace C N|Erickson R E|Laurents D V | [{"numValue":2.76,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"diglycine","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"... | [{"datasets":[],"id":78750,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78751,"numValue":2.62,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78752,"numValue":1.61,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78753,"numValue":null,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:14112 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,112 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,704 | ProTherm | 2.98 | Fluorescence | Urea | diglycine | 100 mM | 20 | null | null | 4.55 | null | null | null | null | 1.39 | 3.28 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1389 | ARTICLE | Urea denaturation of barnase: pH dependence and characterization of the unfolded state. | 1,992 | 10.1021/bi00125a013 | 1547213 | Biochemistry;31;2728-34 | 3 | Pace C N|Erickson R E|Laurents D V | [{"numValue":2.98,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"diglycine","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":... | [{"datasets":[],"id":78754,"numValue":4.55,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78755,"numValue":3.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78756,"numValue":1.39,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78757,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14113 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,113 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,705 | ProTherm | 2.5 | Fluorescence | Urea | diglycine | 100 mM | 20 | null | null | 1.66 | null | null | null | null | 0.52 | 3.22 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1389 | ARTICLE | Urea denaturation of barnase: pH dependence and characterization of the unfolded state. | 1,992 | 10.1021/bi00125a013 | 1547213 | Biochemistry;31;2728-34 | 3 | Pace C N|Erickson R E|Laurents D V | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"diglycine","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"... | [{"datasets":[],"id":78758,"numValue":1.66,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78759,"numValue":3.22,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78760,"numValue":0.52,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78761,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:14114 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,114 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,813 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 52.25 | null | null | null | null | null | 137.2 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":82131,"numValue":52.25,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":82132,"numValue":137.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":82133,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14115 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,115 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,885 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | 14 | null | null | null | null | 5.5 | 2.5 | null | null | null | null | null | null | null | Yes | DG|M|CM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85222,"numValue":14.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":85223,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":85224,"numValue":5.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":85225,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:14117 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,117 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,887 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | 12.8 | null | null | null | null | 5.1 | 2.5 | null | null | null | null | null | null | null | Yes | DG|M|CM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85230,"numValue":12.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":85231,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":85232,"numValue":5.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":85233,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:14118 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,118 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,888 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | 10.2 | null | null | null | null | 3.1 | 3 | null | null | null | null | null | null | null | Yes | DG|M|CM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85234,"numValue":10.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":85235,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":85236,"numValue":3.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":85237,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:14119 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,119 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,889 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | 3 | null | null | null | null | 2 | 1.5 | null | null | null | null | null | null | null | Yes | DG|M|CM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85238,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":85239,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":85240,"numValue":2.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":85241,"numValue":null,"references":[],"str... | |||||||||||||||||||||||
fireprotdb:14120 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,120 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,890 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | 2.2 | null | null | null | null | 1.7 | 1.3 | null | null | null | null | null | null | null | Yes | DG|M|CM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85242,"numValue":2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":85243,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":85244,"numValue":1.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":85245,"numValue":null,"references":[],"str... | |||||||||||||||||||||||
fireprotdb:14121 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,121 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,891 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | 2.2 | null | null | null | null | 1.4 | 1.5 | null | null | null | null | null | null | null | Yes | DG|M|CM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85246,"numValue":2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":85247,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":85248,"numValue":1.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":85249,"numValue":null,"references":[],"str... | |||||||||||||||||||||||
fireprotdb:14122 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,122 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,892 | ProTherm | 5 | Fluorescence | Urea | Sodium acetate | 20 mM | null | NaCl | 0.1 M | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Yes | REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":85250,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14123 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,123 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,893 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 54.9 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85251,"numValue":54.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85252,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14124 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,124 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,894 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 55.7 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85253,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85254,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14125 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,125 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,895 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 53.3 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85255,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85256,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14126 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,126 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,896 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 40.2 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85257,"numValue":40.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85258,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,127 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,897 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 30.2 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85259,"numValue":30.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85260,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,128 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,898 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 31.9 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85261,"numValue":31.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85262,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,129 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,899 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 26.2 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85263,"numValue":26.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85264,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,130 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,900 | ProTherm | 5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 35.6 | 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 | 1711 | ARTICLE | Structural and thermodynamic analysis of a conformationally strained circular permutant of barnase. | 2,009 | 10.1021/bi900039e | 19260676 | Biochemistry;48;3497-507 | 5 | Butler James S|Mitrea Diana M|Mitrousis Gregory|Cingolani Gino|Loh Stewart N | [{"numValue":5.0,"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":"NaCl","type":"ION"}... | [{"datasets":[],"id":85265,"numValue":35.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":85266,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:14131 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,131 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,955 | ProTherm | 8 | CD | Urea | Tris-HCl | 25 mM | 25 | null | null | 7.58 | null | null | null | null | null | 1.84 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1829 | ARTICLE | Measuring the stability of partly folded proteins using TMAO. | 2,003 | 10.1110/ps.0372903 | 12824497 | Protein Sci;12;1522-9 | 2 | Barrick Doug|Mello Cecilia C | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":91229,"numValue":7.58,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91230,"numValue":1.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":91231,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,132 | train | sequence | 302 | 302 | -1 | 157 | -1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,965 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | null | null | 9.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":91264,"numValue":9.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91265,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14133 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,133 | train | mutant | 3,705 | 302 | 4,156 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51V | I51V | 1 | 1 | 0 | 0 | 51 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 51 | A | L | false | false | 60.198183 | 21.51375 | 8,511 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I4V | null | null | null | 0.67 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":28921,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28922,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,134 | train | mutant | 3,705 | 302 | 4,156 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51V | I51V | 1 | 1 | 0 | 0 | 51 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 51 | A | L | false | false | 60.198183 | 21.51375 | 8,649 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I4V | null | null | null | 0.67 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":29352,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29353,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14135 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,135 | train | mutant | 3,705 | 302 | 4,156 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51V | I51V | 1 | 1 | 0 | 0 | 51 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 51 | A | L | false | false | 60.198183 | 21.51375 | 9,809 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I4V | null | null | 8.01 | 0.81 | null | null | null | 4.2 | 1.88 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33624,"numValue":8.01,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33625,"numValue":0.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33626,"numValue":1.88,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33627,"numValue":4.2... | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14136 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,136 | train | mutant | 3,784 | 302 | 4,240 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A | I51A | 1 | 1 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51 | A | L | false | false | 60.198183 | 21.51375 | 8,650 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I4A | null | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":29354,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29355,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14137 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,137 | train | mutant | 3,784 | 302 | 4,240 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A | I51A | 1 | 1 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51 | A | L | false | false | 60.198183 | 21.51375 | 8,651 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I4A | null | null | null | 0.83 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["SAAFEC_S983.csv"],"id":29356,"numValue":0.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29357,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,138 | train | mutant | 3,784 | 302 | 4,240 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A | I51A | 1 | 1 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51 | A | L | false | false | 60.198183 | 21.51375 | 9,810 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I4A | null | null | 8.07 | 0.75 | null | null | null | 3.8 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33629,"numValue":8.07,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33630,"numValue":0.75,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33631,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33632,"numValue":3.8,"references":[],"... | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14139 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,139 | train | mutant | 6,895 | 302 | 7,537 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A|I98V | I51A|I98V | 2 | 2 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51|98 | A | L|E | true | false | 30.350361 | 15.67625 | 14,731 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 20 mM | null | KCl | 200 mM | 1BNI_A:I4A 1BNI_A:I51V | 25.45 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 911 | ARTICLE | The A-state of barnase. | 1,994 | 10.1021/bi00203a015 | 7727370 | Biochemistry;33;11189-99 | 3 | Johnson C M|Fersht A R|Sanz J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"... | [{"datasets":[],"id":54476,"numValue":25.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54477,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,140 | train | mutant | 6,895 | 302 | 7,537 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A|I98V | I51A|I98V | 2 | 2 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51|98 | A | L|E | true | false | 30.350361 | 15.67625 | 14,732 | ProTherm | 2.7 | CD | Thermal | glycine-HCl | 20 mM | null | KCl | 200 mM | 1BNI_A:I4A 1BNI_A:I51V | 25.7 | 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|_PDB_CHAIN_MUTATION | 911 | ARTICLE | The A-state of barnase. | 1,994 | 10.1021/bi00203a015 | 7727370 | Biochemistry;33;11189-99 | 3 | Johnson C M|Fersht A R|Sanz J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"n... | [{"datasets":[],"id":54478,"numValue":25.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54479,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14141 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,141 | train | mutant | 6,895 | 302 | 7,537 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A|I98V | I51A|I98V | 2 | 2 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51|98 | A | L|E | true | false | 30.350361 | 15.67625 | 15,347 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | NaCl | 0.15 M | 1BNI_A:I4A 1BNI_A:I51V | null | null | 6.16 | 2.63 | null | null | null | 2.92 | 2.11 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 713 | ARTICLE | Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. | 1,993 | 10.1021/bi00212a026 | 8257694 | Biochemistry;32;13584-92 | 2 | Fersht A R|Sanz J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56330,"numValue":6.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56331,"numValue":2.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56332,"numValue":2.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56333,"numValue":2.92,"references":[],... | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,142 | train | mutant | 7,117 | 302 | 7,770 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A|I123V | I51A|I123V | 2 | 2 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51|123 | A | L | false | false | 30.099092 | 14.278125 | 15,345 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | NaCl | 0.15 M | 1BNI_A:I4A 1BNI_A:I76V | null | null | 6.93 | 1.86 | null | null | null | 3.61 | 1.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 713 | ARTICLE | Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. | 1,993 | 10.1021/bi00212a026 | 8257694 | Biochemistry;32;13584-92 | 2 | Fersht A R|Sanz J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56320,"numValue":6.93,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56321,"numValue":1.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56322,"numValue":1.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56323,"numValue":3.61,"references":[],... | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14143 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,143 | train | mutant | 7,118 | 302 | 7,771 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I51A|Y125F | I51A|Y125F | 2 | 2 | 0 | 0 | 51 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 51|125 | A | L | true | true | 35.080417 | 15.104375 | 15,346 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | NaCl | 0.15 M | 1BNI_A:I4A 1BNI_A:Y78F | null | null | 6.26 | 2.53 | null | null | null | 3.21 | 1.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 713 | ARTICLE | Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. | 1,993 | 10.1021/bi00212a026 | 8257694 | Biochemistry;32;13584-92 | 2 | Fersht A R|Sanz J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56325,"numValue":6.26,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56326,"numValue":2.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56327,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56328,"numValue":3.21,"references":[],... | [{"id":20365,"numValue":7.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20439,"numValue":8.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,145 | train | mutant | 3,706 | 302 | 4,157 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N52A | N52A | 1 | 1 | 0 | 0 | 52 | N | A | 6 | CONSERVATION | 1BNI | 159 | null | 52 | A | L | false | false | 15.525525 | 17.44 | 8,512 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:N5A | null | null | null | 1.85 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":28923,"numValue":1.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28924,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20366,"numValue":6.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14146 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,146 | train | mutant | 3,706 | 302 | 4,157 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N52A | N52A | 1 | 1 | 0 | 0 | 52 | N | A | 6 | CONSERVATION | 1BNI | 159 | null | 52 | A | L | false | false | 15.525525 | 17.44 | 8,652 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:N5A | null | null | null | 2.06 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":29358,"numValue":2.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29359,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20366,"numValue":6.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14147 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,147 | train | mutant | 3,706 | 302 | 4,157 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N52A | N52A | 1 | 1 | 0 | 0 | 52 | N | A | 6 | CONSERVATION | 1BNI | 159 | null | 52 | A | L | false | false | 15.525525 | 17.44 | 9,811 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N5A | null | null | 7.23 | 1.59 | null | null | null | 3.6 | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33634,"numValue":7.23,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33635,"numValue":1.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33636,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33637,"numValue":3.6,"... | [{"id":20366,"numValue":6.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14148 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,148 | train | mutant | 3,694 | 302 | 4,145 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53A | T53A | 1 | 1 | 0 | 0 | 53 | T | A | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 8,499 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T6A | null | null | null | 2.15 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":28897,"numValue":2.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28898,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14149 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,149 | train | mutant | 3,694 | 302 | 4,145 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53A | T53A | 1 | 1 | 0 | 0 | 53 | T | A | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,637 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6A | null | null | null | 2.53 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":33093,"numValue":2.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33094,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14150 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,150 | train | mutant | 3,694 | 302 | 4,145 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53A | T53A | 1 | 1 | 0 | 0 | 53 | T | A | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,679 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:T6A | null | null | null | 2.23 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 651 | ARTICLE | Mapping the transition state and pathway of protein folding by protein engineering. | 1,989 | 10.1038/340122a0 | 2739734 | Nature;340;122-6 | 4 | Matouschek A|Serrano L|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv"],"id":33244,"numValue":2.23,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33245,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,151 | train | mutant | 3,694 | 302 | 4,145 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53A | T53A | 1 | 1 | 0 | 0 | 53 | T | A | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,813 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T6A | null | null | 6.8 | 2.02 | null | null | null | 3.4 | 1.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33644,"numValue":6.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33645,"numValue":2.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33646,"numValue":1.97,"r... | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14152 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,152 | train | mutant | 3,695 | 302 | 4,146 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53G | T53G | 1 | 1 | 0 | 0 | 53 | T | G | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 8,500 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T6G | null | null | null | 1.21 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":28899,"numValue":1.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28900,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14153 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,153 | train | mutant | 3,695 | 302 | 4,146 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53G | T53G | 1 | 1 | 0 | 0 | 53 | T | G | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,638 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6G | null | null | null | 1.34 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":33095,"numValue":1.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33096,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,154 | train | mutant | 3,695 | 302 | 4,146 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53G | T53G | 1 | 1 | 0 | 0 | 53 | T | G | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,812 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T6G | null | null | 8.21 | 0.61 | null | null | null | 3.9 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33639,"numValue":8.21,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33640,"numValue":0.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33641,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33642,"numValue":3.9,"references":[],"... | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14155 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,155 | train | mutant | 3,908 | 302 | 4,410 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53P | T53P | 1 | 1 | 0 | 0 | 53 | T | P | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,078 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:T6P | null | null | 5.5 | 3.3 | null | null | null | 2.99 | 1.83 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30830,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30831,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30832,"numValue":1.83,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30833,"numValue":2.99,... | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,156 | train | mutant | 4,209 | 302 | 4,714 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53S | T53S | 1 | 1 | 0 | 0 | 53 | T | S | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,636 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6S | null | null | null | 0.22 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":33091,"numValue":0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33092,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,157 | train | mutant | 4,210 | 302 | 4,715 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53N | T53N | 1 | 1 | 0 | 0 | 53 | T | N | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,639 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6N | null | null | null | 1.27 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33097,"numValue":1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33098,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14158 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,158 | train | mutant | 4,211 | 302 | 4,716 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53D | T53D | 1 | 1 | 0 | 0 | 53 | T | D | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,640 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6D | null | null | null | -0.11 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33099,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33100,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14159 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,159 | train | mutant | 4,212 | 302 | 4,717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53Q | T53Q | 1 | 1 | 0 | 0 | 53 | T | Q | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,641 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6Q | null | null | null | 1.87 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33101,"numValue":1.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33102,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,160 | train | mutant | 4,213 | 302 | 4,718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53E | T53E | 1 | 1 | 0 | 0 | 53 | T | E | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 9,642 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T6E | null | null | null | 0.27 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33103,"numValue":0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33104,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,161 | train | mutant | 4,578 | 302 | 5,098 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53H | T53H | 1 | 1 | 0 | 0 | 53 | T | H | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 10,766 | ProTherm | 4.4 | NMR | Urea | Sodium acetate | 30 mM | 25 | NaCl | 1 M | 1BNI_A:T6H | null | null | 5.48 | 2.65 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFE... | [{"datasets":[],"id":37027,"numValue":5.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":37028,"numValue":2.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37029,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14162 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,162 | train | mutant | 4,578 | 302 | 5,098 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T53H | T53H | 1 | 1 | 0 | 0 | 53 | T | H | 4 | CONSERVATION | 1BNI | 159 | null | 53 | A | S | false | false | 71.375589 | 15.794286 | 10,770 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | 1BNI_A:T6H | null | null | 6.49 | 1.56 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":8.9,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":37039,"numValue":6.49,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":37040,"numValue":1.56,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37041,"numValue":null,"references":[],"strValue":"Unknown","type":"... | [{"id":20367,"numValue":4.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,163 | train | mutant | 4,191 | 302 | 4,696 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | F54L | F54L | 1 | 1 | 0 | 0 | 54 | F | L | 6 | CONSERVATION | 1BNI | 159 | null | 54 | A | H | false | false | 29.647283 | 10.720909 | 9,570 | ProTherm | 6.15 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:F7L | null | null | 6.4 | 4.1 | null | null | null | 2.42 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 645 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 1,988 | 10.1038/333784a0 | 3386721 | Nature;333;784-6 | 4 | Nyberg K|Fersht A R|Kellis J T|Sali D | [{"numValue":6.15,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFF... | [{"datasets":[],"id":32768,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":32769,"numValue":4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":32770,"numValue":2.42,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":32771,"numValue":null... | [{"id":20368,"numValue":6.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14164 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,164 | train | mutant | 283 | 302 | 315 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A | D55A | 1 | 1 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 498 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:D8A | 49.72 | -1.91 | null | null | 124.4 | null | 127.3 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"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":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"},{"numValue":null,"strV... | [{"datasets":["HotMuSiC_S1626.csv"],"id":2011,"numValue":49.72,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":2012,"numValue":-1.91,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":2013,"numValue":124.4,... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14165 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,165 | train | mutant | 283 | 302 | 315 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A | D55A | 1 | 1 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 8,781 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:D8A | null | null | 7.97 | 0.69 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":29675,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29676,"numValue":7.97,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","SAAFEC_S983.csv"],"id":29677,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[]... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,166 | train | mutant | 283 | 302 | 315 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A | D55A | 1 | 1 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 9,814 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D8A | null | null | 7.97 | 0.85 | null | null | null | 4.1 | 1.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33649,"numValue":7.97,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":33650,"numValue":0.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33651,"numValue":1.94,"references":[]... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14167 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,167 | train | mutant | 283 | 302 | 315 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A | D55A | 1 | 1 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 11,103 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D8A | null | null | null | 0.99 | null | null | null | 4.12 | null | null | null | null | null | null | null | null | yes | DDG|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","SAAFEC_S1262.csv"],"id":38228,"numValue":0.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38229,"numValue":4.12,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38230,"numValue":null,"references":[],"strValue":"yes",... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14168 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,168 | train | mutant | 283 | 302 | 315 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A | D55A | 1 | 1 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 11,336 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D8A | null | null | 8.94 | 0.99 | null | null | null | 4.12 | 2.15 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":39026,"numValue":8.94,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","SAAFEC_S1262.csv"],"id":39027,"numValue":0.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39028,"numValue":2.15,"references":[],"strValue":null,"... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,169 | train | mutant | 3,909 | 302 | 4,411 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55G | D55G | 1 | 1 | 0 | 0 | 55 | D | G | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 9,079 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D8G | null | null | 7.5 | 1.3 | null | null | null | 3.97 | 1.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30835,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30836,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30837,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30838,"numValue":3.97,... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14170 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,170 | train | mutant | 3,910 | 302 | 4,412 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55S | D55S | 1 | 1 | 0 | 0 | 55 | D | S | 4 | CONSERVATION | 1BNI | 159 | null | 55 | A | H | false | false | 86.605659 | 19.875 | 9,080 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D8S | null | null | 8.1 | 0.7 | null | null | null | 4.07 | 1.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30840,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30841,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30842,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30843,"numValue":4.07,... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,171 | train | mutant | 7,043 | 302 | 7,696 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|D59A | D55A|D59A | 2 | 2 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|59 | A | H | false | false | 82.438633 | 20.5825 | 15,238 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D8A 1BNI_A:D12A | null | null | 7.41 | 1.41 | null | null | null | 4.16 | 1.78 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":55923,"numValue":7.41,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55924,"numValue":1.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55925,"numValue":1.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55926,"numValue":4.16,"references":[],... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14172 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,172 | train | mutant | 7,043 | 302 | 7,696 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|D59A | D55A|D59A | 2 | 2 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|59 | A | H | false | false | 82.438633 | 20.5825 | 15,399 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D8A 1BNI_A:D12A | null | null | null | 0.89 | null | null | null | 4.16 | null | null | null | null | null | null | null | null | yes | DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56527,"numValue":0.89,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56528,"numValue":4.16,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56529,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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