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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:6776 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,776 | train | mutant | 1,255 | 117 | 1,405 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123V | T123V | 1 | 1 | 0 | 0 | 123 | T | V | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 2,419 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41V | 55.4 | 2.7 | null | null | null | null | 94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S2204.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S2204.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8886,"numValue":5... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,777 | train | mutant | 1,255 | 117 | 1,405 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123V | T123V | 1 | 1 | 0 | 0 | 123 | T | V | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 2,514 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41V | 57.2 | 4.2 | null | null | null | null | 94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":9266,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":9267,"numValue":4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9268,"numValue":94.0,"references":[],"strValue":null,"type"... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,778 | train | mutant | 1,255 | 117 | 1,405 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123V | T123V | 1 | 1 | 0 | 0 | 123 | T | V | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,521 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T41V | null | null | 6.4 | -0.8 | null | null | null | 0.98 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49948,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49949,"numValue":-0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49950,"numValue":0.97,"references":[],"strValue":n... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,779 | train | mutant | 1,263 | 117 | 1,413 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123C | T123C | 1 | 1 | 0 | 0 | 123 | T | C | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 2,427 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41C | 54 | 1.3 | null | null | null | null | 93 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":8918,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":8919,"numValue":1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":8920... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,780 | train | mutant | 1,263 | 117 | 1,413 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123C | T123C | 1 | 1 | 0 | 0 | 123 | T | C | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 2,522 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41C | 55.9 | 2.9 | null | null | null | null | 91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9298,"numValue":55.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9299,"numValue":2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9300,"numValue":91.0,"references":[],"strValue":null,"type":"DHVH"... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,784 | train | mutant | 1,270 | 117 | 1,420 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123I | T123I | 1 | 1 | 0 | 0 | 123 | T | I | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 4,337 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41I | 57.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 415 | ARTICLE | Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability. | 2,000 | 10.1006/jmbi.2000.4140 | 11023780 | J Mol Biol;303;125-30 | 4 | Chen J|Lu Z|Sakon J|Stites W E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":16059,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":16060,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,785 | train | mutant | 1,270 | 117 | 1,420 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123I | T123I | 1 | 1 | 0 | 0 | 123 | T | I | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 12,780 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T41I | null | null | 6.1 | -0.7 | null | null | null | 1 | 6.14 | 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 | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46427,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46428,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46429,"numValue":6.14,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46430,"numValue":1.0,... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6786 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,786 | train | mutant | 1,270 | 117 | 1,420 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123I | T123I | 1 | 1 | 0 | 0 | 123 | T | I | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,622 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T41I | null | null | 6.1 | 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|_PDB_CHAIN_MUTATION | 415 | ARTICLE | Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability. | 2,000 | 10.1006/jmbi.2000.4140 | 11023780 | J Mol Biol;303;125-30 | 4 | Chen J|Lu Z|Sakon J|Stites W E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50399,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":50400,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,787 | train | mutant | 6,173 | 117 | 6,761 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123G | T123G | 1 | 1 | 0 | 0 | 123 | T | G | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,089 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T41G | null | null | 3.5 | 2 | null | null | null | 0.57 | 0.9 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47914,"numValue":3.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47915,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47916,"numValue":0.9,"references":[],"strValue":nul... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,788 | train | mutant | 6,174 | 117 | 6,762 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123A | T123A | 1 | 1 | 0 | 0 | 123 | T | A | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,090 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T41A | null | null | 5.5 | 0 | null | null | null | 0.82 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47919,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47920,"numValue":0.0,"refer... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,789 | train | mutant | 6,209 | 117 | 6,803 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123E | T123E | 1 | 1 | 0 | 0 | 123 | T | E | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,197 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:T41E | null | null | 7.3 | 2.1 | null | null | null | 1.6 | 4.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":3.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48367,"numValue":7.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48368,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48369,"numValue":4.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48370,"numValue":1.6,"references":[],"str... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,790 | train | mutant | 6,209 | 117 | 6,803 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123E | T123E | 1 | 1 | 0 | 0 | 123 | T | E | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,198 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:T41E | null | null | 9.2 | 2.6 | null | null | null | 1.8 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48372,"numValue":9.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48373,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48374,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48375,"numValue":1.8,"references":[],"str... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,791 | train | mutant | 6,209 | 117 | 6,803 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123E | T123E | 1 | 1 | 0 | 0 | 123 | T | E | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,199 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:T41E | null | null | 8.7 | 3 | null | null | null | 1.6 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48377,"numValue":8.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":48378,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48379,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48380,"numValue":1.6,"re... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,792 | train | mutant | 6,209 | 117 | 6,803 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123E | T123E | 1 | 1 | 0 | 0 | 123 | T | E | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,200 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:T41E | null | null | 7.6 | 4.3 | null | null | null | 1.5 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48382,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48383,"numValue":4.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48384,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48385,"numValue":1.5,"references":[],"str... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,793 | train | mutant | 6,209 | 117 | 6,803 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123E | T123E | 1 | 1 | 0 | 0 | 123 | T | E | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,201 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:T41E | null | null | 7.6 | 4 | null | null | null | 1.4 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48387,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48388,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48389,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48390,"numValue":1.4,"references":[],"str... | [{"id":36,"numValue":null,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7893,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,795 | train | mutant | 6,118 | 117 | 6,706 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | P124A | P124A | 1 | 1 | 0 | 0 | 124 | P | A | 9 | CONSERVATION | 1STN | 140 | null | 124 | A | L | true | false | 16.843378 | 16.404286 | 13,029 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:P42A | null | null | 5.6 | -0.1 | null | null | null | 0.84 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47616,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47617,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47618,"numValue":0.98,"reference... | [{"id":7894,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,796 | train | mutant | 7,193 | 117 | 7,848 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L|P124G | H206L|P124G | 2 | 2 | 0 | 0 | 206 | H | L | 9 | CONSERVATION | 1STN | 140 | null | 124|206 | A | L|H | true | false | 55.944426 | 20.989643 | 15,498 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21 | 1STN_A:P42G 1STN_A:H124L | null | null | null | null | null | null | null | 0.75 | null | null | null | null | null | null | null | null | yes | CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 816 | ARTICLE | High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. | 1,996 | 10.1021/bi952012g | 8620010 | Biochemistry;35;3857-64 | 4 | Markley J L|Truckses D M|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":21.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"... | [{"datasets":[],"id":56904,"numValue":0.75,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56905,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7894,"numValue":9.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:6798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,798 | train | mutant | 5,961 | 117 | 6,531 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E125G | E125G | 1 | 1 | 0 | 0 | 125 | E | G | 9 | ACTIVE_SITE|CONSERVATION | 1STN | 140 | null | 125 | A | L | false | true | 42.347284 | 23.772222 | 12,831 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E43G | null | null | 6.1 | -0.5 | null | null | null | 0.9 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46671,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46672,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46673,"numValue":0.97,"reference... | [{"id":32,"numValue":null,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7895,"numValue":9.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,799 | train | mutant | 6,332 | 117 | 6,932 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E125D | E125D | 1 | 1 | 0 | 0 | 125 | E | D | 9 | ACTIVE_SITE|CONSERVATION | 1STN | 140 | null | 125 | A | L | false | true | 42.347284 | 23.772222 | 13,472 | ProTherm | 7 | Fluorescence | GdnHCl | Potassium phosphate | 20 | NaCl | 100 mM | 1STN_A:E43D | null | null | 5.7 | -0.2 | null | null | null | 0.92 | 0.96 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 851 | ARTICLE | Deletion of the omega-loop in the active site of staphylococcal nuclease. 1. Effect on catalysis and stability. | 1,991 | 10.1021/bi00229a005 | 2015219 | Biochemistry;30;3621-7 | 6 | Poole L B|Loveys D A|Hale S P|Gerlt J A|Stanczyk S M|Bolton P H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"NaCl... | [{"datasets":[],"id":49707,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49708,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49709,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":497... | [{"id":32,"numValue":null,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7895,"numValue":9.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6800 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,800 | train | mutant | 1,248 | 117 | 1,398 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126S | T126S | 1 | 1 | 0 | 0 | 126 | T | S | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,412 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44S | 52.2 | -0.5 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":8858,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":8859,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":8860,"numValue":89... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,801 | train | mutant | 1,248 | 117 | 1,398 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126S | T126S | 1 | 1 | 0 | 0 | 126 | T | S | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,507 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44S | 53.3 | 0.3 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S499.csv|EASE-MM_S1676.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":9238,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv","Saraboji_S1... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,802 | train | mutant | 1,248 | 117 | 1,398 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126S | T126S | 1 | 1 | 0 | 0 | 126 | T | S | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 13,514 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T44S | null | null | 5.6 | 0 | null | null | null | 0.84 | 0.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49913,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49914,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49915,"numValue":0... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,803 | train | mutant | 1,256 | 117 | 1,406 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126V | T126V | 1 | 1 | 0 | 0 | 126 | T | V | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,420 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44V | 52.2 | -0.5 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|HotMuSiC_S1626.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8890,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8891,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","HotMuSiC_S1626.csv","Saraboji... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,804 | train | mutant | 1,256 | 117 | 1,406 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126V | T126V | 1 | 1 | 0 | 0 | 126 | T | V | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,515 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44V | 54 | 1 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9270,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9271,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9272,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9273,"numValue":null,"references":[],"s... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,805 | train | mutant | 1,256 | 117 | 1,406 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126V | T126V | 1 | 1 | 0 | 0 | 126 | T | V | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 13,522 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T44V | null | null | 5.7 | -0.1 | null | null | null | 0.84 | 1 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49953,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49954,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49955,"numValue":1.0,"references... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,806 | train | mutant | 1,264 | 117 | 1,414 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126C | T126C | 1 | 1 | 0 | 0 | 126 | T | C | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,428 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44C | 52.4 | -0.3 | null | null | null | null | 83 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8922,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8923,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"da... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,808 | train | mutant | 1,264 | 117 | 1,414 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126C | T126C | 1 | 1 | 0 | 0 | 126 | T | C | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 13,530 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T44C | null | null | 5.4 | 0.2 | null | null | null | 0.85 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49993,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49994,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49995,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4999... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,809 | train | mutant | 1,271 | 117 | 1,421 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126I | T126I | 1 | 1 | 0 | 0 | 126 | T | I | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,435 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44I | 48.5 | -4.2 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8950,"numValue":48.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8951,"numValue":-4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":895... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,810 | train | mutant | 1,271 | 117 | 1,421 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126I | T126I | 1 | 1 | 0 | 0 | 126 | T | I | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 2,530 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T44I | 49.7 | -3.3 | null | null | null | null | 78 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|EASE-MM_S238.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["Broom_S605.csv","PoPMuSiC-2.0_S2648.csv"],"id":9330,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","EASE-MM_S238.csv"],"id":9331,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv"],"id":9332,"numValue":78.0,"references":... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,811 | train | mutant | 1,271 | 117 | 1,421 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126I | T126I | 1 | 1 | 0 | 0 | 126 | T | I | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 12,781 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T44I | null | null | 4.8 | 0.6 | null | null | null | 0.74 | 6.48 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46432,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46433,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46434,"numValue":6.48,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4643... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,812 | train | mutant | 6,175 | 117 | 6,763 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126G | T126G | 1 | 1 | 0 | 0 | 126 | T | G | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 13,091 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T44G | null | null | 4.9 | 0.6 | null | null | null | 0.78 | 0.93 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47924,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47925,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47926,"numValue":0.93,"references... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,813 | train | mutant | 6,176 | 117 | 6,764 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T126A | T126A | 1 | 1 | 0 | 0 | 126 | T | A | 8 | CONSERVATION | 1STN | 140 | null | 126 | A | S | false | false | 28.690511 | 23.717143 | 13,092 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T44A | null | null | 5.1 | 0.4 | null | null | null | 0.79 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47929,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47930,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47931,"numValue":0.96,"references... | [{"id":7896,"numValue":8.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6814 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,814 | train | mutant | 5,990 | 117 | 6,560 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K127A | K127A | 1 | 1 | 0 | 0 | 127 | K | A | 7 | CONSERVATION | 1STN | 140 | null | 127 | A | S | false | true | 124.863388 | 40.317778 | 12,864 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K45A | null | null | 5.9 | -0.3 | null | null | null | 0.81 | 1.05 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46836,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46837,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46838,"numValue":1.05,"reference... | [{"id":7897,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,816 | train | mutant | 5,991 | 117 | 6,561 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K127G | K127G | 1 | 1 | 0 | 0 | 127 | K | G | 7 | CONSERVATION | 1STN | 140 | null | 127 | A | S | false | true | 124.863388 | 40.317778 | 12,865 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K45G | null | null | 5.8 | -0.2 | null | null | null | 0.83 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46841,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46842,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46843,"numValue":1.01,"reference... | [{"id":7897,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,817 | train | mutant | 5,991 | 117 | 6,561 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K127G | K127G | 1 | 1 | 0 | 0 | 127 | K | G | 7 | CONSERVATION | 1STN | 140 | null | 127 | A | S | false | true | 124.863388 | 40.317778 | 13,583 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K45G | null | null | 5.6 | -0.2 | null | null | null | 0.83 | 1.01 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50245,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50246,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50247,"numValue":1.01,"reference... | [{"id":7897,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6818 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,818 | train | mutant | 1,791 | 117 | 2,005 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H128Y | H128Y | 1 | 1 | 0 | 0 | 128 | H | Y | 8 | CONSERVATION | 1STN | 140 | null | 128 | A | B | false | true | 42.990021 | 42.437 | 3,443 | ProTherm | 5.38 | NMR | Thermal | Unknown | null | NaCl | 0.3 M | 1STN_A:H46Y | 47.2 | -0.6 | null | null | null | null | 69.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.38,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.3 M","type":"ION_CONC"},{"numVa... | [{"datasets":["AUTOMUTE_S1962.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12724,"numValue":47.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","capriotti_S1615_map.csv"... | [{"id":7898,"numValue":8.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6819 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,819 | train | mutant | 1,791 | 117 | 2,005 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H128Y | H128Y | 1 | 1 | 0 | 0 | 128 | H | Y | 8 | CONSERVATION | 1STN | 140 | null | 128 | A | B | false | true | 42.990021 | 42.437 | 8,091 | ProTherm | 5.38 | NMR | Thermal | Unknown | 40 | NaCl | 0.3 M | 1STN_A:H46Y | null | null | 1.4 | 0 | null | 0 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.38,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27508,"numValue":0.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27509,"numValue":1.4,"refere... | [{"id":7898,"numValue":8.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,820 | train | mutant | 6,025 | 117 | 6,595 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H128A | H128A | 1 | 1 | 0 | 0 | 128 | H | A | 8 | CONSERVATION | 1STN | 140 | null | 128 | A | B | false | true | 42.990021 | 42.437 | 12,900 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:H46A | null | null | 5.1 | 0.5 | null | null | null | 0.74 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47016,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47017,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47018,"numValue":0.98,"references... | [{"id":7898,"numValue":8.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,821 | train | mutant | 6,026 | 117 | 6,596 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H128G | H128G | 1 | 1 | 0 | 0 | 128 | H | G | 8 | CONSERVATION | 1STN | 140 | null | 128 | A | B | false | true | 42.990021 | 42.437 | 12,901 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:H46G | null | null | 5.2 | 0.4 | null | null | null | 0.81 | 0.93 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47021,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47022,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47023,"numValue":0.93,"references... | [{"id":7898,"numValue":8.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6822 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,822 | train | mutant | 1,278 | 117 | 1,428 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | P129F | P129F | 1 | 1 | 0 | 0 | 129 | P | F | 7 | CONSERVATION | 1STN | 140 | null | 129 | A | T | false | true | 119.718743 | 41.308571 | 2,442 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:P47F | 51.8 | -0.9 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8978,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8979,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8980,"numValue":85.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8981,"numValue":null,"references":[],"... | [{"id":7899,"numValue":7.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6823 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,823 | train | mutant | 1,278 | 117 | 1,428 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | P129F | P129F | 1 | 1 | 0 | 0 | 129 | P | F | 7 | CONSERVATION | 1STN | 140 | null | 129 | A | T | false | true | 119.718743 | 41.308571 | 2,537 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:P47F | 52.8 | -0.2 | null | null | null | null | 83 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9358,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9359,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_... | [{"id":7899,"numValue":7.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,824 | train | mutant | 1,278 | 117 | 1,428 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | P129F | P129F | 1 | 1 | 0 | 0 | 129 | P | F | 7 | CONSERVATION | 1STN | 140 | null | 129 | A | T | false | true | 119.718743 | 41.308571 | 13,337 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 600 mM | 1STN_A:P47F | null | null | 5.2 | 0.3 | null | null | null | 0.83 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49040,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49041,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49042,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4904... | [{"id":7899,"numValue":7.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,826 | train | mutant | 6,120 | 117 | 6,708 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | P129A | P129A | 1 | 1 | 0 | 0 | 129 | P | A | 7 | CONSERVATION | 1STN | 140 | null | 129 | A | T | false | true | 119.718743 | 41.308571 | 13,031 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:P47A | null | null | 4.9 | 0.6 | null | null | null | 0.79 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47626,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47627,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47628,"numValue":0.92,"references... | [{"id":7899,"numValue":7.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,827 | train | mutant | 7,194 | 117 | 7,849 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L|P129G | H206L|P129G | 2 | 2 | 0 | 0 | 206 | H | L | 7 | CONSERVATION | 1STN | 140 | null | 129|206 | A | T|H | false | true | 107.382109 | 33.441786 | 15,499 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21 | 1STN_A:P47G 1STN_A:H124L | null | null | 2.8 | null | null | null | null | 0.75 | 5.7 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 816 | ARTICLE | High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. | 1,996 | 10.1021/bi952012g | 8620010 | Biochemistry;35;3857-64 | 4 | Markley J L|Truckses D M|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":21.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"... | [{"datasets":[],"id":56906,"numValue":2.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56907,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56908,"numValue":0.75,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56909,"numValue":null,"references":[],"st... | [{"id":7899,"numValue":7.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:6828 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,828 | train | mutant | 7,196 | 117 | 7,851 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L|P129G|P199G | H206L|P129G|P199G | 3 | 3 | 0 | 0 | 206 | H | L | 7 | CONSERVATION | 1STN | 140 | null | 129|199|206 | A | T|H | true | true | 92.54994 | 29.729286 | 15,501 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21 | 1STN_A:P47G 1STN_A:P117G 1STN_A:H124L | null | null | 3.47 | null | null | null | null | 0.75 | 5.28 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 816 | ARTICLE | High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. | 1,996 | 10.1021/bi952012g | 8620010 | Biochemistry;35;3857-64 | 4 | Markley J L|Truckses D M|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":21.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"... | [{"datasets":[],"id":56914,"numValue":3.47,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56915,"numValue":5.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56916,"numValue":0.75,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56917,"numValue":null,"references":[],"... | [{"id":7899,"numValue":7.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7969,"numValue":7.0,"position":199,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRang... | |||||||||||||
fireprotdb:6829 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,829 | train | mutant | 1,279 | 117 | 1,429 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K130F | K130F | 1 | 1 | 0 | 0 | 130 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 130 | A | T | false | false | 191.830475 | 58.938889 | 2,443 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K48F | 52.3 | -0.4 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8982,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8983,"numValue":-0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8984,"numValue":84.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8985,"numValue":null,"references":[],"... | [{"id":7900,"numValue":5.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6831 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,831 | train | mutant | 1,279 | 117 | 1,429 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K130F | K130F | 1 | 1 | 0 | 0 | 130 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 130 | A | T | false | false | 191.830475 | 58.938889 | 13,338 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K48F | null | null | 5 | 0.5 | null | null | null | 0.83 | 0.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49045,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49046,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49047,"numValue":0.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4904... | [{"id":7900,"numValue":5.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,832 | train | mutant | 5,992 | 117 | 6,562 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K130A | K130A | 1 | 1 | 0 | 0 | 130 | K | A | 5 | CONSERVATION | 1STN | 140 | null | 130 | A | T | false | false | 191.830475 | 58.938889 | 12,866 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K48A | null | null | 5.7 | -0.1 | null | null | null | 0.81 | 1.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46846,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46847,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46848,"numValue":1.03,"reference... | [{"id":7900,"numValue":5.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6833 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,833 | train | mutant | 5,993 | 117 | 6,563 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K130G | K130G | 1 | 1 | 0 | 0 | 130 | K | G | 5 | CONSERVATION | 1STN | 140 | null | 130 | A | T | false | false | 191.830475 | 58.938889 | 12,867 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K48G | null | null | 5.8 | -0.2 | null | null | null | 0.84 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46851,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46852,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46853,"numValue":1.01,"reference... | [{"id":7900,"numValue":5.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6834 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,834 | train | mutant | 6,047 | 117 | 6,632 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K130E | K130E | 1 | 1 | 0 | 0 | 130 | K | E | 5 | CONSERVATION | 1STN | 140 | null | 130 | A | T | false | false | 191.830475 | 58.938889 | 12,924 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K48E | null | null | 5.4 | 0 | null | null | null | 0.85 | 6.34 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47136,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47137,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47138,"numValue":6... | [{"id":7900,"numValue":5.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6835 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,835 | train | mutant | 6,048 | 117 | 6,633 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K130Q | K130Q | 1 | 1 | 0 | 0 | 130 | K | Q | 5 | CONSERVATION | 1STN | 140 | null | 130 | A | T | false | false | 191.830475 | 58.938889 | 12,925 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K48Q | null | null | 5.3 | 0.1 | null | null | null | 0.83 | 6.47 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47141,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47142,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47143,"numValue":6.47,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4714... | [{"id":7900,"numValue":5.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,836 | train | mutant | 1,280 | 117 | 1,430 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K131F | K131F | 1 | 1 | 0 | 0 | 131 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 131 | A | T | true | false | 140.966577 | 54.694445 | 2,444 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K49F | 51.5 | -1.2 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv|EASE-MM_S238.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":8986,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":8987,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S238.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id"... | [{"id":7901,"numValue":7.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,837 | train | mutant | 1,280 | 117 | 1,430 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K131F | K131F | 1 | 1 | 0 | 0 | 131 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 131 | A | T | true | false | 140.966577 | 54.694445 | 2,539 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K49F | 52.2 | -0.8 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv","STRUM_Q3421.csv"],"id":9366,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv","STRUM_Q3421.csv"],"id":9367,"numValue":-0.8,"references":[],"strValue":null,"t... | [{"id":7901,"numValue":7.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,838 | train | mutant | 1,280 | 117 | 1,430 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K131F | K131F | 1 | 1 | 0 | 0 | 131 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 131 | A | T | true | false | 140.966577 | 54.694445 | 13,339 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K49F | null | null | 5.5 | 0 | null | null | null | 0.89 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49050,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49051,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49052,"numValue":0... | [{"id":7901,"numValue":7.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,839 | train | mutant | 5,994 | 117 | 6,564 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K131A | K131A | 1 | 1 | 0 | 0 | 131 | K | A | 7 | CONSERVATION | 1STN | 140 | null | 131 | A | T | true | false | 140.966577 | 54.694445 | 12,868 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K49A | null | null | 5.3 | 0.3 | null | null | null | 0.77 | 0.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46856,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46857,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46858,"numValue":0.99,"references... | [{"id":7901,"numValue":7.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,841 | train | mutant | 5,995 | 117 | 6,565 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K131G | K131G | 1 | 1 | 0 | 0 | 131 | K | G | 7 | CONSERVATION | 1STN | 140 | null | 131 | A | T | true | false | 140.966577 | 54.694445 | 12,869 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K49G | null | null | 5.4 | 0.2 | null | null | null | 0.8 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46861,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46862,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46863,"numValue":0.97,"references... | [{"id":7901,"numValue":7.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,842 | train | mutant | 5,995 | 117 | 6,565 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K131G | K131G | 1 | 1 | 0 | 0 | 131 | K | G | 7 | CONSERVATION | 1STN | 140 | null | 131 | A | T | true | false | 140.966577 | 54.694445 | 13,581 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K49G | null | null | 5.2 | 0.2 | null | null | null | 0.8 | 0.97 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50235,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50236,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50237,"numValue":0.97,"references... | [{"id":7901,"numValue":7.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,844 | train | mutant | 2,161 | 117 | 2,455 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G132C | G132C | 1 | 1 | 0 | 0 | 132 | G | C | 4 | CONSERVATION | 1STN | 140 | null | 132 | A | B | false | false | 28.07812 | 39.5875 | 13,603 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G50C | null | null | 4.7 | 0.8 | null | null | null | 0.73 | 6.42 | 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 | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50313,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50314,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50315,"numValue":6.42,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50316,"numValue":0.73,... | [{"id":7902,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,845 | train | mutant | 2,169 | 117 | 2,463 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G132F | G132F | 1 | 1 | 0 | 0 | 132 | G | F | 4 | CONSERVATION | 1STN | 140 | null | 132 | A | B | false | false | 28.07812 | 39.5875 | 4,263 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:G50F | 50.5 | -2.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":15803,"numValue":50.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15804,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15805,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7902,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,846 | train | mutant | 2,169 | 117 | 2,463 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G132F | G132F | 1 | 1 | 0 | 0 | 132 | G | F | 4 | CONSERVATION | 1STN | 140 | null | 132 | A | B | false | false | 28.07812 | 39.5875 | 13,340 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G50F | null | null | 4.7 | 0.8 | null | null | null | 0.75 | 0.94 | 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 | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49055,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":49056,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49057,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49058,"numValue":0.75,"references":[],"s... | [{"id":7902,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6848 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,848 | train | mutant | 6,128 | 117 | 6,716 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G132A | G132A | 1 | 1 | 0 | 0 | 132 | G | A | 4 | CONSERVATION | 1STN | 140 | null | 132 | A | B | false | false | 28.07812 | 39.5875 | 13,040 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G50A | null | null | 5.7 | -0.2 | null | null | null | 0.81 | 1.04 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | EXP_TEMPERATURE|PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47671,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47672,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47673,"numValue":1.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":476... | [{"id":7902,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,849 | train | mutant | 6,128 | 117 | 6,716 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G132A | G132A | 1 | 1 | 0 | 0 | 132 | G | A | 4 | CONSERVATION | 1STN | 140 | null | 132 | A | B | false | false | 28.07812 | 39.5875 | 13,589 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G50A | null | null | 5.7 | -0.3 | null | null | null | 0.81 | 1.04 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50275,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50276,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50277,"numValue":1.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":502... | [{"id":7902,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,850 | train | mutant | 6,129 | 117 | 6,717 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G132V | G132V | 1 | 1 | 0 | 0 | 132 | G | V | 4 | CONSERVATION | 1STN | 140 | null | 132 | A | B | false | false | 28.07812 | 39.5875 | 13,041 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G50V | null | null | 4.4 | 1.1 | null | null | null | 0.67 | 0.96 | 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 | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47676,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47677,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47678,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47679,"numValue":0.67,... | [{"id":7902,"numValue":4.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6851 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,851 | train | mutant | 1,219 | 117 | 1,369 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133T | V133T | 1 | 1 | 0 | 0 | 133 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 2,382 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V51T | 51.7 | -1 | null | null | null | null | 95 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv"],"id":8738,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8739,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8740,"numValue":95.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,852 | train | mutant | 1,219 | 117 | 1,369 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133T | V133T | 1 | 1 | 0 | 0 | 133 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 2,477 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V51T | 53.5 | 0.5 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9118,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9119,"numValue":0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6853 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,853 | train | mutant | 1,219 | 117 | 1,369 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133T | V133T | 1 | 1 | 0 | 0 | 133 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 13,480 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51T | null | null | 5.8 | -0.2 | null | null | null | 0.86 | 1 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49746,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49747,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49748,"numValue":1.0,"references... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,854 | train | mutant | 1,227 | 117 | 1,377 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133S | V133S | 1 | 1 | 0 | 0 | 133 | V | S | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 2,390 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V51S | 52.1 | -0.6 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8770,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,855 | train | mutant | 1,227 | 117 | 1,377 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133S | V133S | 1 | 1 | 0 | 0 | 133 | V | S | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 2,485 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V51S | 53.5 | 0.5 | null | null | null | null | 90 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":9150,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":9151,"numValue":0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Sarab... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,856 | train | mutant | 1,227 | 117 | 1,377 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133S | V133S | 1 | 1 | 0 | 0 | 133 | V | S | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 13,489 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51S | null | null | 5.5 | 0.1 | null | null | null | 0.85 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49791,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49792,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49793,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4979... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,857 | train | mutant | 5,888 | 117 | 6,458 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133I | V133I | 1 | 1 | 0 | 0 | 133 | V | I | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 12,730 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51I | null | null | 5.5 | -0.1 | null | null | null | 0.83 | 6.54 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46177,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46178,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46179,"numValue":6.54,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":461... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6858 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,858 | train | mutant | 5,889 | 117 | 6,459 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133L | V133L | 1 | 1 | 0 | 0 | 133 | V | L | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 12,731 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51L | null | null | 5.2 | 0.2 | null | null | null | 0.82 | 6.28 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46182,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46183,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46184,"numValue":6.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4618... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,859 | train | mutant | 6,294 | 117 | 6,894 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133A | V133A | 1 | 1 | 0 | 0 | 133 | V | A | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 13,424 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51A | null | null | 5.18 | 0.3 | null | null | null | 0.8 | 0.93 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 850 | ARTICLE | Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. | 1,990 | 10.1021/bi00487a007 | 2261461 | Biochemistry;29;8033-41 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49468,"numValue":5.18,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49469,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49470,"numValue":0.93,"reference... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,860 | train | mutant | 6,294 | 117 | 6,894 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133A | V133A | 1 | 1 | 0 | 0 | 133 | V | A | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 13,564 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51A | null | null | 5.2 | 0.2 | null | null | null | 0.82 | 0.95 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50150,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50151,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50152,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5015... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6862 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,862 | train | mutant | 6,295 | 117 | 6,895 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V133G | V133G | 1 | 1 | 0 | 0 | 133 | V | G | 7 | CONSERVATION | 1STN | 140 | null | 133 | A | S | false | false | 96.838852 | 33.111428 | 13,565 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V51G | null | null | 5.1 | 0.3 | null | null | null | 0.8 | 0.96 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50155,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50156,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50157,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5015... | [{"id":7903,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,863 | train | mutant | 1,281 | 117 | 1,431 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E134F | E134F | 1 | 1 | 0 | 0 | 134 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 134 | A | L | true | false | 38.47219 | 29.788889 | 2,445 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E52F | 52.2 | -0.5 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8990,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8991,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8992,"numValue":84.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8993,"numValue":null,"references":[],"... | [{"id":7904,"numValue":8.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,864 | train | mutant | 1,281 | 117 | 1,431 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E134F | E134F | 1 | 1 | 0 | 0 | 134 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 134 | A | L | true | false | 38.47219 | 29.788889 | 2,540 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E52F | 53 | 0 | null | null | null | null | 81 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9370,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9371,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9... | [{"id":7904,"numValue":8.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,865 | train | mutant | 1,281 | 117 | 1,431 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E134F | E134F | 1 | 1 | 0 | 0 | 134 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 134 | A | L | true | false | 38.47219 | 29.788889 | 13,341 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 600 mM | 1STN_A:E52F | null | null | 4.8 | 0.7 | null | null | null | 0.78 | 0.94 | 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 | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49060,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49061,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49062,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49063,"numValue":0.78,... | [{"id":7904,"numValue":8.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,866 | train | mutant | 5,962 | 117 | 6,532 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E134A | E134A | 1 | 1 | 0 | 0 | 134 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 134 | A | L | true | false | 38.47219 | 29.788889 | 12,832 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E52A | null | null | 5.5 | 0.1 | null | null | null | 0.8 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46676,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46677,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46678,"numValue":0.98,"references... | [{"id":7904,"numValue":8.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,868 | train | mutant | 5,963 | 117 | 6,533 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E134G | E134G | 1 | 1 | 0 | 0 | 134 | E | G | 8 | CONSERVATION | 1STN | 140 | null | 134 | A | L | true | false | 38.47219 | 29.788889 | 12,833 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E52G | null | null | 5.2 | 0.4 | null | null | null | 0.78 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46681,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46682,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46683,"numValue":0.95,"references... | [{"id":7904,"numValue":8.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6869 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,869 | train | mutant | 5,963 | 117 | 6,533 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E134G | E134G | 1 | 1 | 0 | 0 | 134 | E | G | 8 | CONSERVATION | 1STN | 140 | null | 134 | A | L | true | false | 38.47219 | 29.788889 | 13,579 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E52G | null | null | 5 | 0.4 | null | null | null | 0.78 | 0.95 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50225,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50226,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50227,"numValue":0.95,"references... | [{"id":7904,"numValue":8.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,870 | train | mutant | 5,996 | 117 | 6,566 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K135A | K135A | 1 | 1 | 0 | 0 | 135 | K | A | 7 | CONSERVATION | 1STN | 140 | null | 135 | A | T | true | false | 156.537852 | 38.042222 | 12,870 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K53A | null | null | 5.2 | 0.2 | null | null | null | 0.78 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46866,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46867,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46868,"numValue":0.96,"references... | [{"id":7905,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6872 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,872 | train | mutant | 1,231 | 117 | 1,381 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136F | Y136F | 1 | 1 | 0 | 0 | 136 | Y | F | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 2,394 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y54F | 50.9 | -1.8 | null | null | null | null | 81 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8786,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8787,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S1676.csv"],"id":8788,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1925.csv","EASE... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,873 | train | mutant | 1,231 | 117 | 1,381 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136F | Y136F | 1 | 1 | 0 | 0 | 136 | Y | F | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 2,489 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y54F | 52.8 | -0.2 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9166,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9167,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9168,"numValue":82.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9169,"numValue":null,"references":[],"... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,874 | train | mutant | 1,231 | 117 | 1,381 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136F | Y136F | 1 | 1 | 0 | 0 | 136 | Y | F | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 13,497 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y54F | null | null | 5.1 | 0.5 | null | null | null | 0.79 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49831,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49832,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49833,"numValue":0.96,"references... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,876 | train | mutant | 1,237 | 117 | 1,387 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136L | Y136L | 1 | 1 | 0 | 0 | 136 | Y | L | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 2,495 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y54L | 41 | -12 | null | null | null | null | 55 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9190,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9191,"numValue":-12.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9192,"numValue":55.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9193,"numValue":null,"references":[],... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,877 | train | mutant | 1,237 | 117 | 1,387 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136L | Y136L | 1 | 1 | 0 | 0 | 136 | Y | L | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 13,504 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y54L | null | null | 2.2 | 3.4 | null | null | null | 0.35 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49863,"numValue":2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49864,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49865,"numValue":0.95,"references":[],"strValue":nu... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,878 | train | mutant | 6,322 | 117 | 6,922 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136A | Y136A | 1 | 1 | 0 | 0 | 136 | Y | A | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 13,458 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y54A | null | null | 3.28 | 2.2 | null | null | null | 0.5 | 0.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 850 | ARTICLE | Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. | 1,990 | 10.1021/bi00487a007 | 2261461 | Biochemistry;29;8033-41 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49637,"numValue":3.28,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49638,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49639,"numValue":0.89,"references":[],"strValue":n... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6879 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,879 | train | mutant | 6,322 | 117 | 6,922 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y136A | Y136A | 1 | 1 | 0 | 0 | 136 | Y | A | 6 | CONSERVATION | 1STN | 140 | null | 136 | A | T | true | false | 47.0813 | 25.445834 | 13,558 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y54A | null | null | 3.3 | 2.1 | null | null | null | 0.54 | 0.89 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50120,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50121,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50122,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50123,"numValue":0.54,... | [{"id":7906,"numValue":6.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,882 | train | mutant | 6,130 | 117 | 6,718 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G137A | G137A | 1 | 1 | 0 | 0 | 137 | G | A | 8 | CONSERVATION | 1STN | 140 | null | 137 | A | H | false | false | 0 | 17.1275 | 13,042 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G55A | null | null | 4.9 | 0.6 | null | null | null | 0.76 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47681,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47682,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47683,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4768... | [{"id":7907,"numValue":8.0,"position":137,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,884 | train | mutant | 6,121 | 117 | 6,709 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | P138G | P138G | 1 | 1 | 0 | 0 | 138 | P | G | 5 | CONSERVATION | 1STN | 140 | null | 138 | A | H | false | false | 64.677231 | 16.098572 | 13,032 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:P56G | null | null | 4.5 | 1 | null | null | null | 0.72 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47631,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47632,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47633,"numValue":0.92,"references":[],"strValue":nu... | [{"id":7908,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,886 | train | mutant | 1,282 | 117 | 1,432 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139F | E139F | 1 | 1 | 0 | 0 | 139 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 2,446 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E57F | 51.6 | -1.1 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8994,"numValue":51.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8995,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8996,"numValue":85.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8997,"numValue":null,"references":[],"... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,887 | train | mutant | 1,282 | 117 | 1,432 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139F | E139F | 1 | 1 | 0 | 0 | 139 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 2,541 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E57F | 52.4 | -0.6 | null | null | null | null | 80 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9374,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":9375,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"d... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,888 | train | mutant | 1,282 | 117 | 1,432 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139F | E139F | 1 | 1 | 0 | 0 | 139 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 4,264 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E57F | 52.4 | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":15806,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15807,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15808,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6889 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,889 | train | mutant | 1,282 | 117 | 1,432 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139F | E139F | 1 | 1 | 0 | 0 | 139 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 13,342 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 600 mM | 1STN_A:E57F | null | null | 4.8 | 0.7 | null | null | null | 0.72 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49065,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":49066,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49067,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49068,"numValue":0.72,"... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,890 | train | mutant | 1,282 | 117 | 1,432 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139F | E139F | 1 | 1 | 0 | 0 | 139 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 13,613 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E57F | null | null | 4.6 | 0.9 | null | null | null | 0.72 | 6.28 | 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 | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50363,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50364,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50365,"numValue":6.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50366,"numValue":0.72,... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,891 | train | mutant | 2,162 | 117 | 2,456 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139C | E139C | 1 | 1 | 0 | 0 | 139 | E | C | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 4,255 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E57C | 52.1 | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":15779,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15780,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15781,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,892 | train | mutant | 2,162 | 117 | 2,456 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139C | E139C | 1 | 1 | 0 | 0 | 139 | E | C | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 13,604 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E57C | null | null | 4.8 | 0.7 | null | null | null | 0.75 | 6.39 | 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 | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50318,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50319,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50320,"numValue":6.39,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50321,"numValue":0.75,... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,893 | train | mutant | 5,964 | 117 | 6,534 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139A | E139A | 1 | 1 | 0 | 0 | 139 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 12,834 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E57A | null | null | 5.4 | 0.2 | null | null | null | 0.8 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46686,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46687,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46688,"numValue":0.97,"references... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,895 | train | mutant | 6,049 | 117 | 6,634 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E139K | E139K | 1 | 1 | 0 | 0 | 139 | E | K | 8 | CONSERVATION | 1STN | 140 | null | 139 | A | H | true | false | 88.794398 | 19.948889 | 12,926 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E57K | null | null | 5.3 | 0.1 | null | null | null | 0.84 | 6.27 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47146,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47147,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47148,"numValue":6.27,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4714... | [{"id":7909,"numValue":8.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,897 | train | mutant | 6,091 | 117 | 6,679 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A140G | A140G | 1 | 1 | 0 | 0 | 140 | A | G | 9 | CONSERVATION | 1STN | 140 | null | 140 | A | H | false | false | 0 | 12.406 | 13,002 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A58G | null | null | 2.9 | 2.6 | null | null | null | 0.44 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47481,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47482,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47483,"numValue":0.98,"references":[],"strValue":nu... | [{"id":7910,"numValue":9.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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