row_id string | dataset_id string | source_dataset string | source_file string | source_table string | source_sha string | row_index int64 | split string | subject_type string | entry_id int64 | sequence_id int64 | target_sequence_id int64 | source_sequence_length int64 | target_sequence_length int64 | protein_id int64 | protein_name string | organism string | isoform int64 | protein_ids string | protein_names string | organisms string | isoforms string | uniprot_accessions string | interpro_accessions string | ec_numbers string | megascale_ids string | other_references string | mutations string | substitutions string | deletions string | insertions string | mutation_count int64 | substitution_count int64 | deletion_count int64 | insertion_count int64 | first_position int64 | first_source_aa string | first_target_aa string | conservation float64 | feature_types string | pdb_ids string | afdb_ids string | structure_ids string | structure_methods string | structure_resolution_min float64 | residue_positions string | residue_chain_names string | residue_secondary_structures string | residue_in_pocket_any bool | residue_in_tunnel_any bool | residue_asa_mean float64 | residue_bfactor_mean float64 | experiment_id int64 | experiment_dataset string | ph float64 | measure string | method string | buffer string | buffer_conc string | exp_temperature float64 | ion string | ion_conc string | pdb_chain_mutation string | tm float64 | dtm float64 | dg float64 | dg_text string | ddg float64 | dh float64 | dcp float64 | dhvh float64 | cm float64 | m_value float64 | trypsin_ml float64 | chymotrypsin_ml float64 | stabilizing float64 | stabilizing_text string | domainome_fitness float64 | domainome_fitness_std float64 | domainome_ddg float64 | domainome_ddg_std float64 | reversibility string | state string | measurement_types string | measurement_datasets string | annotation_types string | publication_id string | publication_type string | publication_title string | publication_year int64 | publication_doi string | publication_pmid string | publication_journal string | publication_url string | publication_author_count int64 | publication_authors string | annotations_json string | measurements_json string | features_json string |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:6668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,668 | train | mutant | 7,198 | 117 | 7,853 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | M114A|T115A | M114A|T115A | 2 | 2 | 0 | 0 | 114 | M | A | 5 | CONSERVATION | 1STN | 140 | null | 114|115 | A | E | true | false | 38.613626 | 19.217768 | 15,503 | ProTherm | 7 | CD | GdnHCl | NaH2PO4 | 10 mM | 20 | NaCl | 100 mM | 1STN_A:M32A 1STN_A:T33A | null | null | null | 3.3 | null | null | null | null | 1.13 | null | null | null | null | null | null | null | Unknown | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 935 | ARTICLE | Structural and energetic differences between insertions and substitutions in staphylococcal nuclease. | 1,992 | 10.1002/prot.340130206 | 1620695 | Proteins;13;132-40 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":56921,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56922,"numValue":1.13,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56923,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7884,"numValue":5.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,669 | train | mutant | 1,246 | 117 | 1,396 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115S | T115S | 1 | 1 | 0 | 0 | 115 | T | S | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 2,410 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33S | 47.2 | -5.5 | 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":8850,"numValue":47.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8851,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8852,"numValue":85.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8853,"numValue":null,"references":[],"... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,671 | train | mutant | 1,246 | 117 | 1,396 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115S | T115S | 1 | 1 | 0 | 0 | 115 | T | S | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,124 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33S | null | null | -1.4 | null | null | null | null | null | 1.07 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"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":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48056,"numValue":-1.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48057,"numValue":1.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48058,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,673 | train | mutant | 1,246 | 117 | 1,396 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115S | T115S | 1 | 1 | 0 | 0 | 115 | T | S | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,512 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33S | null | null | 4.3 | 1.3 | null | null | null | 0.62 | 1.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.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":49903,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":49904,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49905,"nu... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,674 | train | mutant | 1,254 | 117 | 1,404 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115V | T115V | 1 | 1 | 0 | 0 | 115 | T | V | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 2,418 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33V | 53.3 | 0.6 | null | null | null | null | 91 | 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":8882,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8883,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8884... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,675 | train | mutant | 1,254 | 117 | 1,404 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115V | T115V | 1 | 1 | 0 | 0 | 115 | T | V | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 2,513 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33V | 55.3 | 2.3 | null | null | null | null | 89 | 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":9262,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":9263,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":9264,"numValue":89.0,"ref... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,676 | train | mutant | 1,254 | 117 | 1,404 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115V | T115V | 1 | 1 | 0 | 0 | 115 | T | V | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 4,336 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33V | 55.3 | 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":16057,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":16058,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,677 | train | mutant | 1,254 | 117 | 1,404 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115V | T115V | 1 | 1 | 0 | 0 | 115 | T | V | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,520 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33V | null | null | 6 | -0.4 | null | null | null | 0.92 | 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 | 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":49943,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49944,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49945,"numValue":0.98,"reference... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,678 | train | mutant | 1,254 | 117 | 1,404 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115V | T115V | 1 | 1 | 0 | 0 | 115 | T | V | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,621 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33V | null | null | 5.8 | 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":50397,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":50398,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,679 | train | mutant | 1,262 | 117 | 1,412 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115C | T115C | 1 | 1 | 0 | 0 | 115 | T | C | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 2,426 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33C | 49.1 | -3.6 | null | null | null | null | 78 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.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","STRUM_Q3421.csv"],"id":8914,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8915,"numValue":-3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_d... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,680 | train | mutant | 1,262 | 117 | 1,412 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115C | T115C | 1 | 1 | 0 | 0 | 115 | T | C | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 2,521 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33C | 50.7 | -2.3 | null | null | null | null | 74 | 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":9294,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9295,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9296,"numValue":74.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9297,"numValue":null,"references":[],"... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,681 | train | mutant | 1,262 | 117 | 1,412 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115C | T115C | 1 | 1 | 0 | 0 | 115 | T | C | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,528 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33C | null | null | 4.4 | 1.2 | null | null | null | 0.7 | 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 | 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":49983,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49984,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49985,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49986,"numValue":0.7,"... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,683 | train | mutant | 1,269 | 117 | 1,419 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115I | T115I | 1 | 1 | 0 | 0 | 115 | T | I | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 2,528 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T33I | 55.2 | 2.2 | null | null | null | null | 92 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.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":"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"],"id":9322,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","EASE-MM_S238.csv"],"id":9323,"numValue":2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv","EASE-MM_S238.csv"],"id":9324,"numValue":92.0,"references":[],"str... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,684 | train | mutant | 1,269 | 117 | 1,419 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115I | T115I | 1 | 1 | 0 | 0 | 115 | T | I | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 12,779 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33I | null | null | 6 | -0.6 | null | null | null | 0.95 | 6.34 | 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":46422,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46423,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46424,"numValue":6.34,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":464... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,685 | train | mutant | 6,171 | 117 | 6,759 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115G | T115G | 1 | 1 | 0 | 0 | 115 | T | G | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,087 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33G | null | null | 3 | 2.5 | null | null | null | 0.4 | 1.1 | 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 | 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":47904,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47905,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47906,"numValue":1.1,"references":[],"strValue":nul... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,686 | train | mutant | 6,172 | 117 | 6,760 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115A | T115A | 1 | 1 | 0 | 0 | 115 | T | A | 7 | CONSERVATION | 1STN | 140 | null | 115 | A | E | false | false | 36.836368 | 12.604286 | 13,088 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33A | null | null | 4.1 | 1.4 | null | null | null | 0.56 | 1.07 | 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":47909,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47910,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47911,"numValue":1.07,"references":[],"strValue":nu... | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,687 | train | mutant | 7,214 | 117 | 7,869 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T115S|A172S | T115S|A172S | 2 | 2 | 0 | 0 | 115 | T | S | 7 | CONSERVATION | 1STN | 140 | null | 115|172 | A | E | true | false | 18.418184 | 10.210143 | 15,523 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33S 1STN_A:A90S | null | null | null | 3.16 | null | null | null | null | 1.2 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":56983,"numValue":3.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56984,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56985,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,688 | train | mutant | 7,238 | 117 | 7,893 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|T115S | L119A|T115S | 2 | 2 | 0 | 0 | 119 | L | A | 7 | CONSERVATION | 1STN | 140 | null | 115|119 | A | E|T | true | true | 25.136731 | 12.324018 | 15,548 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33S 1STN_A:L37A | null | null | null | 2.21 | null | null | null | null | 1.01 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57058,"numValue":2.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57059,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57060,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,689 | train | mutant | 7,241 | 117 | 7,896 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|T115S | E157V|T115S | 2 | 2 | 0 | 0 | 157 | E | V | 7 | CONSERVATION | 1STN | 140 | null | 115|157 | A | E | true | false | 21.817136 | 12.742698 | 15,551 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T33S 1STN_A:E75V | null | null | null | 3.21 | null | null | null | null | 0.89 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57067,"numValue":3.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57068,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57069,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7885,"numValue":7.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,690 | train | mutant | 148 | 117 | 173 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116C | F116C | 1 | 1 | 0 | 0 | 116 | F | C | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 277 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 1STN_A:F34C | 40 | -13 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"Potassium chloride","ty... | [{"datasets":[],"id":1123,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1124,"numValue":-13.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1125,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,691 | train | mutant | 148 | 117 | 173 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116C | F116C | 1 | 1 | 0 | 0 | 116 | F | C | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 2,894 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 1STN_A:F34C | 40 | -13 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Saraboji_S2204.csv|M47andM8_S1810.csv|M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":... | [{"datasets":["Saraboji_S2204.csv"],"id":10512,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["Saraboji_S2204.csv"],"id":10513,"numValue":-13.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S2204.csv"],"id":10514,"numValue":null... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,692 | train | mutant | 148 | 117 | 173 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116C | F116C | 1 | 1 | 0 | 0 | 116 | F | C | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 12,711 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | 20 | Potassium chloride | 100 mM | 1STN_A:F34C | null | 72 | 2.7 | 2.8 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DTM|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_... | [{"datasets":[],"id":46102,"numValue":72.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":46103,"numValue":2.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46104,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46105,"numValue":null,"references":[],... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,694 | train | mutant | 6,204 | 117 | 6,798 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116E | F116E | 1 | 1 | 0 | 0 | 116 | F | E | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 13,170 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:F34E | null | null | 5.6 | 3.9 | null | null | null | 1.1 | 4.9 | 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":48232,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48233,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48234,"numValue":4.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48235,"numValue":1.1,"references":[],"str... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,695 | train | mutant | 6,204 | 117 | 6,798 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116E | F116E | 1 | 1 | 0 | 0 | 116 | F | E | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 13,171 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:F34E | null | null | 6.4 | 5.4 | null | null | null | 1.1 | 5.6 | 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":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":48237,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48238,"numValue":5.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48239,"numValue":5.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48240,"numValue":1.1,"references":[],"str... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,696 | train | mutant | 6,204 | 117 | 6,798 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116E | F116E | 1 | 1 | 0 | 0 | 116 | F | E | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 13,172 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:F34E | null | null | 5.2 | 6.5 | null | null | null | 0.9 | 5.7 | 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":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":48242,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48243,"numValue":6.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48244,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48245,"numValue":0.9,"references":[],"str... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,697 | train | mutant | 6,204 | 117 | 6,798 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116E | F116E | 1 | 1 | 0 | 0 | 116 | F | E | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 13,173 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:F34E | null | null | 3.8 | 8.1 | null | null | null | 0.7 | 5.6 | 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":7.9,"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":48247,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48248,"numValue":8.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48249,"numValue":5.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48250,"numValue":0.7,"references":[],"str... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,698 | train | mutant | 6,204 | 117 | 6,798 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116E | F116E | 1 | 1 | 0 | 0 | 116 | F | E | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 13,174 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:F34E | null | null | 3.7 | 7.9 | null | null | null | 0.6 | 5.8 | 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":48252,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48253,"numValue":7.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48254,"numValue":5.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48255,"numValue":0.6,"references":[],"str... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,699 | train | mutant | 6,331 | 117 | 6,931 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F116A | F116A | 1 | 1 | 0 | 0 | 116 | F | A | 8 | CONSERVATION | 1STN | 140 | null | 116 | A | E | true | false | 0.134371 | 10.447273 | 13,467 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:F34A | null | null | 1.78 | 3.7 | null | null | null | 0.2 | 1.12 | 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":49682,"numValue":1.78,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49683,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49684,"numValue":1.12,"references":[],"strValue":n... | [{"id":7886,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,700 | train | mutant | 6,031 | 117 | 6,601 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R117A | R117A | 1 | 1 | 0 | 0 | 117 | R | A | 9 | ACTIVE_SITE|CONSERVATION | 1STN | 140 | null | 117 | A | E | true | true | 38.760184 | 11.456364 | 12,906 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R35A | null | null | 4.2 | 1.4 | null | null | null | 0.6 | 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 | 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":47046,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47047,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47048,"numValue":1.01,"references":[],"strValue":nu... | [{"id":31,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7887,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,701 | train | mutant | 6,032 | 117 | 6,602 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R117G | R117G | 1 | 1 | 0 | 0 | 117 | R | G | 9 | ACTIVE_SITE|CONSERVATION | 1STN | 140 | null | 117 | A | E | true | true | 38.760184 | 11.456364 | 12,907 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R35G | null | null | 3.4 | 2.2 | null | null | null | 0.46 | 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 | 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":47051,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47052,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47053,"numValue":1.03,"references":[],"strValue":nu... | [{"id":31,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7887,"numValue":9.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,702 | train | mutant | 149 | 117 | 174 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118C | L118C | 1 | 1 | 0 | 0 | 118 | L | C | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 278 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 1STN_A:L36C | 39 | -14 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"Potassium chloride","ty... | [{"datasets":[],"id":1126,"numValue":39.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1127,"numValue":-14.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1128,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,703 | train | mutant | 149 | 117 | 174 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118C | L118C | 1 | 1 | 0 | 0 | 118 | L | C | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 2,895 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 1STN_A:L36C | 39 | -14 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":... | [{"datasets":[],"id":10515,"numValue":39.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv"],"id":10516,"numValue":-14.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":10517,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERS... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,704 | train | mutant | 149 | 117 | 174 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118C | L118C | 1 | 1 | 0 | 0 | 118 | L | C | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 12,712 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | 20 | Potassium chloride | 100 mM | 1STN_A:L36C | null | 71 | 2.6 | 2.9 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DTM|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_... | [{"datasets":[],"id":46106,"numValue":71.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":46107,"numValue":2.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46108,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46109,"numValue":null,"references":[],... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,705 | train | mutant | 149 | 117 | 174 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118C | L118C | 1 | 1 | 0 | 0 | 118 | L | C | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 12,713 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | 20 | Potassium chloride | 100 mM | 1STN_A:L36C | null | null | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_... | [{"datasets":[],"id":46110,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46111,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,706 | train | mutant | 149 | 117 | 174 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118C | L118C | 1 | 1 | 0 | 0 | 118 | L | C | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 12,714 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | 20 | Potassium chloride | 50 microM pdTp | 1STN_A:L36C | null | null | null | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_... | [{"datasets":[],"id":46112,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46113,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,707 | train | mutant | 149 | 117 | 174 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118C | L118C | 1 | 1 | 0 | 0 | 118 | L | C | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,154 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | 20 | Potassium chloride | 100 mM | 1STN_A:L36C | null | null | 2.6 | null | null | null | 71 | null | null | null | null | null | null | null | null | null | Unknown | DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue"... | [{"datasets":[],"id":48154,"numValue":71.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":48155,"numValue":2.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48156,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,708 | train | mutant | 5,917 | 117 | 6,487 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118I | L118I | 1 | 1 | 0 | 0 | 118 | L | I | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 12,761 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L36I | null | null | 2.3 | 3.1 | null | null | null | 0.35 | 6.64 | 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":46332,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46333,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46334,"numValue":6.64,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46335,"numValue":0.35,... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,710 | train | mutant | 6,190 | 117 | 6,784 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,125 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L36A | null | null | -3.6 | null | null | null | null | null | 1.15 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"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":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48059,"numValue":-3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48060,"numValue":1.15,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48061,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6711 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,711 | train | mutant | 6,190 | 117 | 6,784 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,409 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L36A | null | null | 1.98 | 3.5 | null | null | null | 0.2 | 1.13 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.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":49393,"numValue":1.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49394,"numValue":3.5,"references":[],"strValue":null,"... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,712 | train | mutant | 6,191 | 117 | 6,785 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118G | L118G | 1 | 1 | 0 | 0 | 118 | L | G | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,126 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L36G | null | null | -5.4 | null | null | null | null | null | 1.24 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"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":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48062,"numValue":-5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48063,"numValue":1.24,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48064,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,713 | train | mutant | 6,191 | 117 | 6,785 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118G | L118G | 1 | 1 | 0 | 0 | 118 | L | G | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,410 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L36G | null | null | 0.18 | 5.3 | null | null | null | 0 | 1.23 | 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":49398,"numValue":0.18,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49399,"numValue":5.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49400,"numValue":1.23,"references":[],"strValue":n... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,715 | train | mutant | 6,205 | 117 | 6,799 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118E | L118E | 1 | 1 | 0 | 0 | 118 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,176 | ProTherm | 4.4 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L36E | null | null | 6.9 | 4.2 | null | null | null | 1.3 | 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":4.4,"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":48262,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48263,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48264,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48265,"numValue":1.3,"references":[],"str... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,716 | train | mutant | 6,205 | 117 | 6,799 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118E | L118E | 1 | 1 | 0 | 0 | 118 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,177 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L36E | null | null | 7.2 | 4.6 | null | null | null | 1.3 | 5.4 | 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":48267,"numValue":7.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48268,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48269,"numValue":5.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48270,"numValue":1.3,"references":[],"str... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,717 | train | mutant | 6,205 | 117 | 6,799 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118E | L118E | 1 | 1 | 0 | 0 | 118 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,178 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L36E | null | null | 6.4 | 5.3 | null | null | null | 1.1 | 5.7 | 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":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":48272,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48273,"numValue":5.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48274,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48275,"numValue":1.1,"references":[],"str... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,718 | train | mutant | 6,205 | 117 | 6,799 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118E | L118E | 1 | 1 | 0 | 0 | 118 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,179 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L36E | null | null | 4.4 | 7.5 | null | null | null | 0.7 | 6.1 | 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":7.9,"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":48277,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48278,"numValue":7.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48279,"numValue":6.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48280,"numValue":0.7,"references":[],"str... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,719 | train | mutant | 6,205 | 117 | 6,799 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118E | L118E | 1 | 1 | 0 | 0 | 118 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,180 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L36E | null | null | 3.2 | 8.4 | null | null | null | 0.5 | 6.4 | 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":48282,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48283,"numValue":8.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48284,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48285,"numValue":0.5,"references":[],"str... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,720 | train | mutant | 6,205 | 117 | 6,799 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L118E | L118E | 1 | 1 | 0 | 0 | 118 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 118 | A | E | true | true | 1.092755 | 12.5 | 13,181 | ProTherm | 9.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L36E | null | null | 1.5 | 8.8 | null | null | null | 0.2 | 7.7 | 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":9.9,"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":48287,"numValue":1.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48288,"numValue":8.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48289,"numValue":7.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48290,"numValue":0.2,"references":[],"str... | [{"id":7888,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,721 | train | mutant | 5,919 | 117 | 6,489 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119I | L119I | 1 | 1 | 0 | 0 | 119 | L | I | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 12,763 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37I | null | null | 3.4 | 2 | null | null | null | 0.57 | 6 | 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":46342,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46343,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46344,"numValue":6.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46345,"numValue":0.57,"... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,722 | train | mutant | 5,920 | 117 | 6,490 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119V | L119V | 1 | 1 | 0 | 0 | 119 | L | V | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 12,764 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37V | null | null | 2.4 | 3 | null | null | null | 0.43 | 5.53 | 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":46347,"numValue":2.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46348,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46349,"numValue":5.53,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46350,"numValue":0.43,... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,723 | train | mutant | 6,192 | 117 | 6,786 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A | L119A | 1 | 1 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,127 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A | null | null | -1.8 | null | null | null | null | null | 0.9 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"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":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48065,"numValue":-1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48066,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48067,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,724 | train | mutant | 6,192 | 117 | 6,786 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A | L119A | 1 | 1 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,411 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A | null | null | 3.78 | 1.7 | null | null | null | 0.6 | 0.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.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":49403,"numValue":3.78,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49404,"numValue":1.7,"references":[],"strValue":null,"... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,725 | train | mutant | 6,193 | 117 | 6,787 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119G | L119G | 1 | 1 | 0 | 0 | 119 | L | G | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,128 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37G | null | null | -3.9 | null | null | null | null | null | 0.95 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"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":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48068,"numValue":-3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48069,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48070,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,726 | train | mutant | 6,193 | 117 | 6,787 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119G | L119G | 1 | 1 | 0 | 0 | 119 | L | G | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,412 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37G | null | null | 1.68 | 3.8 | null | null | null | 0.2 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.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":49408,"numValue":1.68,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49409,"numValue":3.8,"references":[],"strValue":null,"... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,727 | train | mutant | 6,206 | 117 | 6,800 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119E | L119E | 1 | 1 | 0 | 0 | 119 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,182 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L37E | null | null | 7.4 | 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":48292,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48293,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48294,"numValue":4.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48295,"numValue":1.6,"references":[],"str... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,728 | train | mutant | 6,206 | 117 | 6,800 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119E | L119E | 1 | 1 | 0 | 0 | 119 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,183 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L37E | null | null | 9.1 | 2.7 | null | null | null | 1.8 | 5.1 | 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":48297,"numValue":9.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48298,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48299,"numValue":5.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48300,"numValue":1.8,"references":[],"str... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,729 | train | mutant | 6,206 | 117 | 6,800 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119E | L119E | 1 | 1 | 0 | 0 | 119 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,184 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L37E | null | null | 8.5 | 3.2 | null | null | null | 1.7 | 5 | 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":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":48302,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48303,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48304,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48305,"numValue":1.7,"references":[],"str... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,730 | train | mutant | 6,206 | 117 | 6,800 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119E | L119E | 1 | 1 | 0 | 0 | 119 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 119 | A | T | true | true | 13.437094 | 12.04375 | 13,185 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L37E | null | null | 8.8 | 3.1 | null | null | null | 1.7 | 5.1 | 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 | 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":48307,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":48308,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48309,"numValue":5.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48310,"numValue":1.7,"r... | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,731 | train | mutant | 7,199 | 117 | 7,854 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|L120A | L119A|L120A | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|120 | A | T | true | true | 12.202798 | 13.580625 | 15,504 | ProTherm | 7 | CD | GdnHCl | NaH2PO4 | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:L38A | null | null | null | 1.8 | null | null | null | null | 0.91 | null | null | null | null | null | null | null | Unknown | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 935 | ARTICLE | Structural and energetic differences between insertions and substitutions in staphylococcal nuclease. | 1,992 | 10.1002/prot.340130206 | 1620695 | Proteins;13;132-40 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":56924,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56925,"numValue":0.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56926,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,732 | train | mutant | 7,223 | 117 | 7,878 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|E157V | L119A|E157V | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|157 | A | T|E | true | true | 10.117499 | 12.46243 | 15,532 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:E75V | null | null | null | 2.47 | null | null | null | null | 0.79 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57010,"numValue":2.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57011,"numValue":0.79,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57012,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,733 | train | mutant | 7,224 | 117 | 7,879 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|G161S | L119A|G161S | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|161 | A | T|S | true | true | 16.196944 | 12.463125 | 15,533 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:G79S | null | null | null | 1.83 | null | null | null | null | 0.87 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57013,"numValue":1.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57014,"numValue":0.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57015,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,734 | train | mutant | 7,225 | 117 | 7,880 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|P199L | L119A|P199L | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|199 | A | T | true | true | 38.161348 | 17.174018 | 15,534 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:P117L | null | null | null | 1.69 | null | null | null | null | 0.85 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57016,"numValue":1.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57017,"numValue":0.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57018,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7969,"numValue":7.0,"position":199,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,736 | train | mutant | 7,239 | 117 | 7,894 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|A151T | L119A|A151T | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|151 | A | T|L | true | true | 19.311871 | 13.934875 | 15,549 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:A69T | null | null | null | 4.13 | null | null | null | null | 1.09 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57061,"numValue":4.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57062,"numValue":1.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57063,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7921,"numValue":6.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,737 | train | mutant | 7,240 | 117 | 7,895 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|A172S | L119A|A172S | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|172 | A | T|E | true | true | 6.718547 | 9.929875 | 15,550 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:A90S | null | null | null | 3.32 | null | null | null | null | 1.02 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57064,"numValue":3.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57065,"numValue":1.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57066,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6738 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,738 | train | mutant | 7,258 | 117 | 7,913 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|I154V | L119A|I154V | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|154 | A | T|E | true | true | 13.421626 | 11.303125 | 15,568 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:I72V | null | null | null | 2.78 | null | null | null | null | 1.01 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57118,"numValue":2.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57119,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57120,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,739 | train | mutant | 7,259 | 117 | 7,914 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|Y167A | L119A|Y167A | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|167 | A | T | true | true | 85.492134 | 15.088542 | 15,569 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:Y85A | null | null | null | 1.98 | null | null | null | null | 0.9 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57121,"numValue":1.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57122,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57123,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,740 | train | mutant | 7,260 | 117 | 7,915 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|I174V | L119A|I174V | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|174 | A | T|E | true | true | 7.188846 | 10.67375 | 15,570 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:I92V | null | null | null | 1.77 | null | null | null | null | 0.99 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57124,"numValue":1.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57125,"numValue":0.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57126,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,741 | train | mutant | 7,261 | 117 | 7,916 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|Y195A | L119A|Y195A | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|195 | A | T|L | true | true | 91.21297 | 22.919375 | 15,571 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:Y113A | null | null | null | 1.46 | null | null | null | null | 0.92 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57127,"numValue":1.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57128,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57129,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7965,"numValue":9.0,"position":195,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,742 | train | mutant | 7,262 | 117 | 7,917 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L119A|A212G | L119A|A212G | 2 | 2 | 0 | 0 | 119 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 119|212 | A | T|H | true | true | 35.219001 | 12.945875 | 15,572 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L37A 1STN_A:A130G | null | null | null | 2.53 | null | null | null | null | 0.89 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|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":57130,"numValue":2.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57131,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57132,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7889,"numValue":9.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7982,"numValue":4.0,"position":212,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,743 | train | mutant | 5,921 | 117 | 6,491 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120I | L120I | 1 | 1 | 0 | 0 | 120 | L | I | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 12,765 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L38I | null | null | 3.3 | 2.1 | null | null | null | 0.51 | 6.47 | 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":46352,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46353,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46354,"numValue":6.47,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46355,"numValue":0.51,... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,744 | train | mutant | 5,922 | 117 | 6,492 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120V | L120V | 1 | 1 | 0 | 0 | 120 | L | V | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 12,766 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L38V | null | null | 5.2 | 0.2 | null | null | null | 0.81 | 6.41 | 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":46357,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46358,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46359,"numValue":6.41,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4636... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6745 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,745 | train | mutant | 6,207 | 117 | 6,801 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120E | L120E | 1 | 1 | 0 | 0 | 120 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,186 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38E | null | null | 8.3 | 1.2 | null | null | null | 1.8 | 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":48312,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48313,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48314,"numValue":4.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48315,"numValue":1.8,"references":[],"str... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,746 | train | mutant | 6,207 | 117 | 6,801 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120E | L120E | 1 | 1 | 0 | 0 | 120 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,187 | ProTherm | 4.5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38E | null | null | 9.3 | 2 | null | null | null | 2 | 4.7 | 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":4.5,"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":48317,"numValue":9.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48318,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48319,"numValue":4.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48320,"numValue":2.0,"references":[],"str... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,747 | train | mutant | 6,207 | 117 | 6,801 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120E | L120E | 1 | 1 | 0 | 0 | 120 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,188 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38E | null | null | 9.5 | 2.3 | null | null | null | 1.9 | 5 | 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":48322,"numValue":9.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48323,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48324,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48325,"numValue":1.9,"references":[],"str... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6748 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,748 | train | mutant | 6,207 | 117 | 6,801 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120E | L120E | 1 | 1 | 0 | 0 | 120 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,189 | ProTherm | 5.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38E | null | null | 8.3 | 3.4 | null | null | null | 1.7 | 4.9 | 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":5.9,"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":48327,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48328,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48329,"numValue":4.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48330,"numValue":1.7,"references":[],"str... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,749 | train | mutant | 6,207 | 117 | 6,801 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120E | L120E | 1 | 1 | 0 | 0 | 120 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,190 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38E | null | null | 6.9 | 4.6 | null | null | null | 1.4 | 5 | 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":7.9,"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":48332,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48333,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48334,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48335,"numValue":1.4,"references":[],"str... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,750 | train | mutant | 6,207 | 117 | 6,801 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120E | L120E | 1 | 1 | 0 | 0 | 120 | L | E | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,191 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38E | null | null | 6.9 | 4.6 | null | null | null | 1.3 | 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":48337,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48338,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48339,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48340,"numValue":1.3,"references":[],"str... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,751 | train | mutant | 6,286 | 117 | 6,886 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120A | L120A | 1 | 1 | 0 | 0 | 120 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,413 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L38A | null | null | 3.78 | 1.7 | null | null | null | 0.6 | 0.94 | 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":49413,"numValue":3.78,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49414,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49415,"numValue":0.94,"references":[],"strValue":n... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,752 | train | mutant | 6,286 | 117 | 6,886 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120A | L120A | 1 | 1 | 0 | 0 | 120 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,556 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L38A | null | null | 3.8 | 1.6 | null | null | null | 0.6 | 0.96 | 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":50110,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50111,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50112,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50113,"numValue":0.6,"... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,753 | train | mutant | 6,287 | 117 | 6,887 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120G | L120G | 1 | 1 | 0 | 0 | 120 | L | G | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,414 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L38G | null | null | 4.88 | 0.6 | null | null | null | 0.8 | 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 | 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":49418,"numValue":4.88,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49419,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49420,"numValue":0.9,"references":[],"strValue":nu... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,754 | train | mutant | 6,287 | 117 | 6,887 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120G | L120G | 1 | 1 | 0 | 0 | 120 | L | G | 9 | CONSERVATION | 1STN | 140 | null | 120 | A | T | true | true | 10.968501 | 15.1175 | 13,557 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L38G | null | null | 4.9 | 0.5 | null | null | null | 0.8 | 0.92 | 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":50115,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50116,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50117,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5011... | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,755 | train | mutant | 7,200 | 117 | 7,855 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L120A|V121A | L120A|V121A | 2 | 2 | 0 | 0 | 120 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 120|121 | A | T|E | true | true | 5.856639 | 14.78875 | 15,505 | ProTherm | 7 | CD | GdnHCl | NaH2PO4 | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L38A 1STN_A:V39A | null | null | null | 4 | null | null | null | null | 0.92 | null | null | null | null | null | null | null | Unknown | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 935 | ARTICLE | Structural and energetic differences between insertions and substitutions in staphylococcal nuclease. | 1,992 | 10.1002/prot.340130206 | 1620695 | Proteins;13;132-40 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":56927,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56928,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56929,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7890,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6756 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,756 | train | mutant | 1,218 | 117 | 1,368 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121T | V121T | 1 | 1 | 0 | 0 | 121 | V | T | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 2,381 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V39T | 45.2 | -7.5 | null | null | null | null | 75 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.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":"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":["Broom_S605.csv","PoPMuSiC-2.0_S2648.csv"],"id":8734,"numValue":45.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv"],"id":8735,"numValue":-7.5,"references":[],"strValue":null,"type":"DTM"},{"... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,757 | train | mutant | 1,218 | 117 | 1,368 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121T | V121T | 1 | 1 | 0 | 0 | 121 | V | T | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 2,476 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V39T | 47 | -6 | null | null | null | null | 73 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | 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":["Broom_S605.csv"],"id":9114,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9115,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9116,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9117,"numValue":null,"... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,758 | train | mutant | 1,218 | 117 | 1,368 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121T | V121T | 1 | 1 | 0 | 0 | 121 | V | T | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,479 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V39T | null | null | 4.3 | 1.3 | null | null | null | 0.56 | 1.08 | 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":49741,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49742,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49743,"numValue":1.08,"references":[],"strValue":nu... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,759 | train | mutant | 1,226 | 117 | 1,376 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121S | V121S | 1 | 1 | 0 | 0 | 121 | V | S | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 2,389 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V39S | 41.7 | -11 | null | null | null | null | 69 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.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":["AUTOMUTE_S1925.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8766,"numValue":41.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOM... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,760 | train | mutant | 1,226 | 117 | 1,376 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121S | V121S | 1 | 1 | 0 | 0 | 121 | V | S | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 2,484 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V39S | 42.4 | -10.6 | null | null | null | null | 66 | 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":9146,"numValue":42.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":9147,"numValue":-10.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,761 | train | mutant | 1,226 | 117 | 1,376 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121S | V121S | 1 | 1 | 0 | 0 | 121 | V | S | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,488 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V39S | null | null | 3.2 | 2.4 | null | null | null | 0.46 | 1.03 | 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 | 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":49786,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49787,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49788,"numValue":1.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49789,"numValue":0.46,... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6762 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,762 | train | mutant | 5,886 | 117 | 6,456 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121I | V121I | 1 | 1 | 0 | 0 | 121 | V | I | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 12,728 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V39I | null | null | 5.5 | -0.1 | null | null | null | 0.84 | 6.61 | 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":46167,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46168,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46169,"numValue":6.61,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":461... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,763 | train | mutant | 5,887 | 117 | 6,457 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121L | V121L | 1 | 1 | 0 | 0 | 121 | V | L | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 12,729 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V39L | null | null | 4.5 | 0.9 | null | null | null | 0.68 | 6.68 | 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":46172,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46173,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46174,"numValue":6.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46175,"numValue":0.68,... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,764 | train | mutant | 6,208 | 117 | 6,802 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121E | V121E | 1 | 1 | 0 | 0 | 121 | V | E | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,192 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V39E | null | null | 5.6 | 3.9 | null | null | null | 1.2 | 4.9 | 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":48342,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48343,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48344,"numValue":4.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48345,"numValue":1.2,"references":[],"str... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,765 | train | mutant | 6,208 | 117 | 6,802 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121E | V121E | 1 | 1 | 0 | 0 | 121 | V | E | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,193 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V39E | null | null | 7.5 | 4.2 | 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":4.9,"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":48347,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48348,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48349,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48350,"numValue":1.4,"references":[],"str... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,767 | train | mutant | 6,208 | 117 | 6,802 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121E | V121E | 1 | 1 | 0 | 0 | 121 | V | E | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,195 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V39E | null | null | 5.3 | 6.6 | null | null | null | 0.9 | 5.9 | 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":7.9,"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":48357,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48358,"numValue":6.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48359,"numValue":5.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48360,"numValue":0.9,"references":[],"str... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,768 | train | mutant | 6,208 | 117 | 6,802 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121E | V121E | 1 | 1 | 0 | 0 | 121 | V | E | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,196 | ProTherm | 9.1 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V39E | null | null | 4.4 | 7.2 | null | null | null | 0.8 | 5.8 | 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":9.1,"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":48362,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48363,"numValue":7.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48364,"numValue":5.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48365,"numValue":0.8,"references":[],"str... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,769 | train | mutant | 6,292 | 117 | 6,892 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121A | V121A | 1 | 1 | 0 | 0 | 121 | V | A | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,422 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V39A | null | null | 3.28 | 2.2 | null | null | null | 0.4 | 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 | 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":49458,"numValue":3.28,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49459,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49460,"numValue":0.99,"references":[],"strValue":n... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,770 | train | mutant | 6,293 | 117 | 6,893 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V121G | V121G | 1 | 1 | 0 | 0 | 121 | V | G | 8 | CONSERVATION | 1STN | 140 | null | 121 | A | E | true | true | 0.744777 | 14.46 | 13,423 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V39G | null | null | 0.78 | 4.7 | null | null | null | 0.1 | 0.79 | 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":49463,"numValue":0.78,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49464,"numValue":4.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49465,"numValue":0.79,"references":[],"strValue":n... | [{"id":7891,"numValue":8.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6771 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,771 | train | mutant | 5,948 | 117 | 6,518 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D122A | D122A | 1 | 1 | 0 | 0 | 122 | D | A | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 122 | A | E | true | true | 65.714067 | 19.685 | 12,816 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D40A | null | null | 5.8 | -0.2 | null | null | null | 0.89 | 0.94 | 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":46596,"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":46597,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46598,"numValue":0.94,"reference... | [{"id":35,"numValue":null,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7892,"numValue":9.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,772 | train | mutant | 5,949 | 117 | 6,519 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D122G | D122G | 1 | 1 | 0 | 0 | 122 | D | G | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 122 | A | E | true | true | 65.714067 | 19.685 | 12,817 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D40G | null | null | 5.1 | 0.5 | null | null | null | 0.76 | 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":46601,"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":46602,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46603,"numValue":0.97,"references... | [{"id":35,"numValue":null,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":7892,"numValue":9.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:6773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,773 | train | mutant | 1,247 | 117 | 1,397 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 2,411 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41S | 49.6 | -3.1 | null | null | null | null | 79 | 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":8854,"numValue":49.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8855,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8856,"numValue":79.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8857,"numValue":null,"references":[],"... | [{"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:6774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,774 | train | mutant | 1,247 | 117 | 1,397 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 2,506 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T41S | 50.6 | -2.4 | null | null | null | null | 72 | 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":9234,"numValue":50.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9235,"numValue":-2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9236,"numValue":72.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9237,"numValue":null,"references":[],"... | [{"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:6775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,775 | train | mutant | 1,247 | 117 | 1,397 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T123S | T123S | 1 | 1 | 0 | 0 | 123 | T | S | 9 | BINDING_SITE|CONSERVATION | 1STN | 140 | null | 123 | A | L | true | false | 10.517511 | 16.144286 | 13,513 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T41S | null | null | 4.5 | 1.1 | null | null | null | 0.73 | 0.92 | 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 | 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":49908,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49909,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49910,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49911,"numValue":0.73,... | [{"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"}] |
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