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:7234 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,234 | train | mutant | 2,165 | 117 | 2,459 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160C | K160C | 1 | 1 | 0 | 0 | 160 | K | C | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 13,607 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K78C | null | null | 5.1 | 0.4 | null | null | null | 0.82 | 6.24 | 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 | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50333,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50334,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50335,"numValue":6.24,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5033... | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,235 | train | mutant | 2,171 | 117 | 2,465 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160F | K160F | 1 | 1 | 0 | 0 | 160 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 4,266 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K78F | 52.5 | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":15812,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15813,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15814,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7236 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,236 | train | mutant | 2,171 | 117 | 2,465 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160F | K160F | 1 | 1 | 0 | 0 | 160 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 13,615 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K78F | null | null | 5.6 | -0.1 | null | null | null | 0.84 | 6.63 | 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 | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50373,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50374,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50375,"numValue":6.63,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":503... | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,238 | train | mutant | 6,007 | 117 | 6,577 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160G | K160G | 1 | 1 | 0 | 0 | 160 | K | G | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 12,881 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K78G | null | null | 4.5 | 1.1 | null | null | null | 0.65 | 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 | 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":46921,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46922,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46923,"numValue":0.99,"references":[],"strValue":nu... | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,239 | train | mutant | 6,064 | 117 | 6,649 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160E | K160E | 1 | 1 | 0 | 0 | 160 | K | E | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 12,941 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K78E | null | null | 4.6 | 0.8 | null | null | null | 0.73 | 6.27 | 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 | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47221,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47222,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47223,"numValue":6.27,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47224,"numValue":0.73,... | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7240 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,240 | train | mutant | 6,065 | 117 | 6,650 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160Q | K160Q | 1 | 1 | 0 | 0 | 160 | K | Q | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 12,942 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K78Q | null | null | 5.3 | 0.1 | null | null | null | 0.79 | 6.67 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47226,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47227,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47228,"numValue":6.67,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4722... | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7241 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,241 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 215 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:G79S | 43.8 | -7.6 | null | null | 65 | 1.96 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":891,"numValue":43.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":892,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":893,"numValue":65.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":89... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7242 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,242 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 221 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:G79S | 38.5 | -8.5 | null | null | 40 | 1.96 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":921,"numValue":38.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":922,"numValue":-8.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":923,"numValue":40.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":92... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,243 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 3,010 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:G79S | 49.7 | -4.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 268 | ARTICLE | Energetics of denaturation and m values of staphylococcal nuclease mutants. | 1,995 | 10.1021/bi00006a025 | 7849061 | Biochemistry;34;2034-41 | 2 | Privalov P L|Carra J H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10921,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10922,"numValue":-4.4,"references":[],"strValue":nul... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7244 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,244 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 3,440 | ProTherm | 5.28 | NMR | Thermal | Unknown | null | NaCl | 0.3 M | 1STN_A:G79S | 38.3 | -9.5 | null | null | null | null | 55 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.28,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.3 M","type":"ION_CONC"},{"numVa... | [{"datasets":["EASE-MM_S1676.csv"],"id":12712,"numValue":38.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12713,"numValue":-9.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12714,"numValue":55.0,"references":[],"strValue":null,"type":"DH... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7245 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,245 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 7,605 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | 51.4 | NaCl | 0.1 M | 1STN_A:G79S | null | null | null | 1.3 | null | 1.96 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":51.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER... | [{"datasets":[],"id":26269,"numValue":1.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26270,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26271,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7246 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,246 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 7,792 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | 47 | NaCl | 0.1 M | 1STN_A:G79S | null | null | null | 1.2 | null | 1.96 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER... | [{"datasets":[],"id":26713,"numValue":1.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26714,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26715,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7247 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,247 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,140 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S | null | null | -2.4 | null | null | null | null | null | 0.92 | 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":48104,"numValue":-2.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48105,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48106,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7248 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,248 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,297 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S | null | null | null | 2.66 | null | null | null | null | 0.82 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | 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":["SAAFEC_S1262.csv"],"id":48857,"numValue":2.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48858,"numValue":0.82,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48859,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,249 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,312 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S | null | null | 3 | 2.6 | null | null | null | 0.5 | 0.89 | 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 | 843 | ARTICLE | Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. | 1,986 | 10.1002/prot.340010113 | 3449854 | Proteins;1;81-9 | 2 | Shortle D|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":48916,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48917,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48918,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48919,"numValue":0.5,"references":[],"st... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,250 | train | mutant | 109 | 117 | 120 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S | G161S | 1 | 1 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,318 | ProTherm | 7 | Fluorescence | Urea | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S | null | null | 3.2 | 2.9 | null | null | null | 1.59 | 0.89 | 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 | 843 | ARTICLE | Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. | 1,986 | 10.1002/prot.340010113 | 3449854 | Proteins;1;81-9 | 2 | Shortle D|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":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","t... | [{"datasets":[],"id":48946,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48947,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48948,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48949,"numValue":1.59,"references":[],"s... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,251 | train | mutant | 6,132 | 117 | 6,720 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161A | G161A | 1 | 1 | 0 | 0 | 161 | G | A | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,044 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79A | null | null | 3.1 | 2.4 | null | null | null | 0.51 | 0.87 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47691,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47692,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47693,"numValue":0.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47694,"numValue":0.51,... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,252 | train | mutant | 6,132 | 117 | 6,720 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161A | G161A | 1 | 1 | 0 | 0 | 161 | G | A | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,588 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79A | null | null | 3.1 | 2.3 | null | null | null | 0.51 | 0.87 | 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":50270,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50271,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50272,"numValue":0.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50273,"numValue":0.51,... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7253 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,253 | train | mutant | 6,133 | 117 | 6,721 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161V | G161V | 1 | 1 | 0 | 0 | 161 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,045 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79V | null | null | 3.1 | 2.4 | null | null | null | 0.5 | 0.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47696,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47697,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47698,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47699,"numValue":0.5,"... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7254 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,254 | train | mutant | 6,240 | 117 | 6,834 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161D | G161D | 1 | 1 | 0 | 0 | 161 | G | D | 6 | CONSERVATION | 1STN | 140 | null | 161 | A | S | true | false | 18.956794 | 12.8825 | 13,296 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79D | null | null | null | 2.28 | null | null | null | null | 0.87 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | 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":["SAAFEC_S1262.csv"],"id":48854,"numValue":2.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48855,"numValue":0.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48856,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,255 | train | mutant | 6,896 | 117 | 7,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|H206L | G161S|H206L | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|206 | A | S|H | true | false | 57.001134 | 19.22875 | 14,733 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:G79S 1STN_A:H124L | 53.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 326 | ARTICLE | Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. | 1,996 | 10.1021/bi960309o | 8756688 | Biochemistry;35;10328-38 | 3 | Hinck A P|Markley J L|Truckses D M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1STN_A:G79S 1STN_A:H124L... | [{"datasets":[],"id":54480,"numValue":53.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54481,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7256 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,256 | train | mutant | 6,896 | 117 | 7,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|H206L | G161S|H206L | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|206 | A | S|H | true | false | 57.001134 | 19.22875 | 14,734 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:G79S 1STN_A:H124L | 43.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 326 | ARTICLE | Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. | 1,996 | 10.1021/bi960309o | 8756688 | Biochemistry;35;10328-38 | 3 | Hinck A P|Markley J L|Truckses D M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1STN_A:G79S 1STN_A:H124L... | [{"datasets":[],"id":54482,"numValue":43.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54483,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,257 | train | mutant | 6,896 | 117 | 7,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|H206L | G161S|H206L | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|206 | A | S|H | true | false | 57.001134 | 19.22875 | 15,110 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | 40 | 1STN_A:G79S 1STN_A:H124L | null | null | 2.85 | null | null | null | 67.3 | null | null | null | null | null | null | null | null | null | yes | DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 326 | ARTICLE | Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. | 1,996 | 10.1021/bi960309o | 8756688 | Biochemistry;35;10328-38 | 3 | Hinck A P|Markley J L|Truckses D M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_C... | [{"datasets":[],"id":55442,"numValue":67.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":55443,"numValue":2.85,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55444,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,258 | train | mutant | 6,896 | 117 | 7,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|H206L | G161S|H206L | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|206 | A | S|H | true | false | 57.001134 | 19.22875 | 15,111 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | 40 | 1STN_A:G79S 1STN_A:H124L | null | null | 0.32 | null | null | null | 33.1 | null | null | null | null | null | null | null | null | null | yes | DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 326 | ARTICLE | Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. | 1,996 | 10.1021/bi960309o | 8756688 | Biochemistry;35;10328-38 | 3 | Hinck A P|Markley J L|Truckses D M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_C... | [{"datasets":[],"id":55445,"numValue":33.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":55446,"numValue":0.32,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55447,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,259 | train | mutant | 6,896 | 117 | 7,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|H206L | G161S|H206L | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|206 | A | S|H | true | false | 57.001134 | 19.22875 | 15,496 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21.5 | 1STN_A:G79S 1STN_A:H124L | null | null | 5.5 | null | null | null | null | 1 | 9.36 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 326 | ARTICLE | Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. | 1,996 | 10.1021/bi960309o | 8756688 | Biochemistry;35;10328-38 | 3 | Hinck A P|Markley J L|Truckses D M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":21.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"... | [{"datasets":[],"id":56896,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56897,"numValue":9.36,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56898,"numValue":1.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56899,"numValue":null,"references":[],"st... | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,261 | train | mutant | 7,231 | 117 | 7,886 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|P199L | G161S|P199L | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|199 | A | S|T | true | false | 40.921198 | 17.593393 | 15,541 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S 1STN_A:P117L | null | null | null | 2.08 | 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":57037,"numValue":2.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57038,"numValue":0.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57039,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7969,"numValue":7.0,"position":199,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,262 | train | mutant | 7,232 | 117 | 7,887 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161D|N200D | G161D|N200D | 2 | 2 | 0 | 0 | 161 | G | D | 6 | CONSERVATION | 1STN | 140 | null | 161|200 | A | S|B | true | true | 14.482784 | 14.293125 | 15,542 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79D 1STN_A:N118D | null | null | null | 2.58 | 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":57040,"numValue":2.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57041,"numValue":0.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57042,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7970,"numValue":8.0,"position":200,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,263 | train | mutant | 7,233 | 117 | 7,888 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|N200D | G161S|N200D | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|200 | A | S|B | true | true | 14.482784 | 14.293125 | 15,543 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S 1STN_A:N118D | null | null | null | 2.79 | null | null | null | null | 0.84 | 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":57043,"numValue":2.79,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57044,"numValue":0.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57045,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7970,"numValue":8.0,"position":200,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,264 | train | mutant | 7,271 | 117 | 7,926 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|Y167A | G161S|Y167A | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|167 | A | S|T | true | true | 88.251984 | 15.507917 | 15,581 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S 1STN_A:Y85A | null | null | null | 2.69 | 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":57157,"numValue":2.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57158,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57159,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,265 | train | mutant | 7,272 | 117 | 7,927 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|I174V | G161S|I174V | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|174 | A | S|E | true | false | 9.948695 | 11.093125 | 15,582 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S 1STN_A:I92V | null | null | null | 2.55 | null | null | null | null | 0.93 | 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":57160,"numValue":2.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57161,"numValue":0.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57162,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7267 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,267 | train | mutant | 7,274 | 117 | 7,929 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|A212G | G161S|A212G | 2 | 2 | 0 | 0 | 161 | G | S | 6 | CONSERVATION | 1STN | 140 | null | 161|212 | A | S|H | true | false | 37.978851 | 13.36525 | 15,584 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G79S 1STN_A:A130G | null | null | null | 3.68 | null | null | null | null | 0.76 | 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":57166,"numValue":3.68,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57167,"numValue":0.76,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57168,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7982,"numValue":4.0,"position":212,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,268 | train | mutant | 1,286 | 117 | 1,436 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q162F | Q162F | 1 | 1 | 0 | 0 | 162 | Q | F | 5 | CONSERVATION | 1STN | 140 | null | 162 | A | L | true | true | 120.357231 | 26.504445 | 2,450 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Q80F | 51.1 | -1.6 | null | null | null | null | 80 | 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":9010,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9011,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9012,"numValue":80.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9013,"numValue":null,"references":[],"... | [{"id":7932,"numValue":5.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,269 | train | mutant | 1,286 | 117 | 1,436 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q162F | Q162F | 1 | 1 | 0 | 0 | 162 | Q | F | 5 | CONSERVATION | 1STN | 140 | null | 162 | A | L | true | true | 120.357231 | 26.504445 | 2,545 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Q80F | 51.7 | -1.3 | null | null | null | null | 80 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | 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":9390,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9391,"numValue":-1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9392,"numValue":80.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"... | [{"id":7932,"numValue":5.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7270 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,270 | train | mutant | 1,286 | 117 | 1,436 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q162F | Q162F | 1 | 1 | 0 | 0 | 162 | Q | F | 5 | CONSERVATION | 1STN | 140 | null | 162 | A | L | true | true | 120.357231 | 26.504445 | 13,352 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q80F | null | null | 4.8 | 0.7 | null | null | null | 0.76 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49115,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49116,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49117,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49118,"numValue":0.76,... | [{"id":7932,"numValue":5.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,272 | train | mutant | 6,154 | 117 | 6,742 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q162A | Q162A | 1 | 1 | 0 | 0 | 162 | Q | A | 5 | CONSERVATION | 1STN | 140 | null | 162 | A | L | true | true | 120.357231 | 26.504445 | 13,067 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q80A | null | null | 5.4 | 0.1 | null | null | null | 0.81 | 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 | 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":47804,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47805,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47806,"numValue":0.97,"references... | [{"id":7932,"numValue":5.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,273 | train | mutant | 6,033 | 117 | 6,603 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R163A | R163A | 1 | 1 | 0 | 0 | 163 | R | A | 4 | CONSERVATION | 1STN | 140 | null | 163 | A | S | true | false | 122.988075 | 25.010909 | 12,908 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R81A | null | null | 4.5 | 1.1 | null | null | null | 0.64 | 1.02 | 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":47056,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47057,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47058,"numValue":1.02,"references":[],"strValue":nu... | [{"id":7933,"numValue":4.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,274 | train | mutant | 6,034 | 117 | 6,604 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R163G | R163G | 1 | 1 | 0 | 0 | 163 | R | G | 4 | CONSERVATION | 1STN | 140 | null | 163 | A | S | true | false | 122.988075 | 25.010909 | 12,909 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R81G | null | null | 3.4 | 2.2 | null | null | null | 0.52 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47061,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47062,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47063,"numValue":0.92,"references":[],"strValue":nu... | [{"id":7933,"numValue":4.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,275 | train | mutant | 1,250 | 117 | 1,400 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164S | T164S | 1 | 1 | 0 | 0 | 164 | T | S | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,414 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82S | 49.2 | -3.5 | null | null | null | null | 79 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|AUTOMUTE_S1925.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | 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":8866,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8867,"numValue":-3.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv"],"id":8868,"numValue":79.0,"references":[],"strValue":null,"type":"DHVH"},... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,276 | train | mutant | 1,250 | 117 | 1,400 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164S | T164S | 1 | 1 | 0 | 0 | 164 | T | S | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,509 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82S | 50.6 | -2.4 | null | null | null | null | 81 | 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":9246,"numValue":50.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":9247,"numValue":-2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":9248,"numValue":81.0,"re... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,277 | train | mutant | 1,250 | 117 | 1,400 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164S | T164S | 1 | 1 | 0 | 0 | 164 | T | S | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 13,516 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T82S | null | null | 4.9 | 0.7 | null | null | null | 0.71 | 1.02 | 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":49923,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49924,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49925,"numValue":1.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49926,"numValue":0.71,... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,279 | train | mutant | 1,258 | 117 | 1,408 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164V | T164V | 1 | 1 | 0 | 0 | 164 | T | V | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,517 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82V | 54.6 | 1.6 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9278,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9279,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9280,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9281,"numValue":null,"references":[],"s... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7280 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,280 | train | mutant | 1,258 | 117 | 1,408 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164V | T164V | 1 | 1 | 0 | 0 | 164 | T | V | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 13,524 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T82V | null | null | 5.8 | -0.2 | null | null | null | 0.87 | 0.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49963,"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":49964,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49965,"numValue":0.99,"reference... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,281 | train | mutant | 1,266 | 117 | 1,416 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164C | T164C | 1 | 1 | 0 | 0 | 164 | T | C | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,430 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82C | 50.2 | -2.5 | null | null | null | null | 87 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|Broom_S605.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1925.csv","Broom_S605.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8930,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,282 | train | mutant | 1,266 | 117 | 1,416 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164C | T164C | 1 | 1 | 0 | 0 | 164 | T | C | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,525 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82C | 51.8 | -1.2 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|EASE-MM_S238.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["Broom_S605.csv","EASE-MM_S238.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv"],"id":9310,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":9311,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUT... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,283 | train | mutant | 1,266 | 117 | 1,416 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164C | T164C | 1 | 1 | 0 | 0 | 164 | T | C | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 13,532 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T82C | null | null | 5.5 | 0.1 | null | null | null | 0.79 | 1.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50003,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50004,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50005,"numValue":1.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5000... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,284 | train | mutant | 1,273 | 117 | 1,423 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164I | T164I | 1 | 1 | 0 | 0 | 164 | T | I | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,437 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82I | 53.5 | 0.8 | null | null | null | null | 90 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.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":8958,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv"],"id":8959,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUT... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,285 | train | mutant | 1,273 | 117 | 1,423 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164I | T164I | 1 | 1 | 0 | 0 | 164 | T | I | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 2,532 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:T82I | 54.6 | 1.6 | null | null | null | null | 92 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9338,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9339,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,286 | train | mutant | 1,273 | 117 | 1,423 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164I | T164I | 1 | 1 | 0 | 0 | 164 | T | I | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 12,783 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T82I | null | null | 5.9 | -0.5 | null | null | null | 0.9 | 6.51 | 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":46442,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46443,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46444,"numValue":6.51,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":464... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,287 | train | mutant | 6,177 | 117 | 6,765 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164G | T164G | 1 | 1 | 0 | 0 | 164 | T | G | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 13,095 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T82G | null | null | 3.5 | 2 | null | null | null | 0.5 | 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 | 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":47944,"numValue":3.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47945,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47946,"numValue":1.01,"references":[],"strValue":nu... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,288 | train | mutant | 6,178 | 117 | 6,766 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T164A | T164A | 1 | 1 | 0 | 0 | 164 | T | A | 6 | CONSERVATION | 1STN | 140 | null | 164 | A | B | true | true | 72.792939 | 15.168571 | 13,096 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T82A | null | null | 4.6 | 0.9 | null | null | null | 0.67 | 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 | 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":47949,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47950,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47951,"numValue":1.01,"references":[],"strValue":nu... | [{"id":7934,"numValue":6.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,289 | train | mutant | 5,950 | 117 | 6,520 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D165A | D165A | 1 | 1 | 0 | 0 | 165 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 165 | A | L | true | true | 35.751861 | 13.31375 | 12,820 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D83A | null | null | 1.8 | 3.8 | null | null | null | 0.27 | 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 | 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":46616,"numValue":1.8,"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":46617,"numValue":3.8,"references":[],"strValue":null,"t... | [{"id":7935,"numValue":9.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,290 | train | mutant | 5,950 | 117 | 6,520 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D165A | D165A | 1 | 1 | 0 | 0 | 165 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 165 | A | L | true | true | 35.751861 | 13.31375 | 13,141 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D83A | null | null | -3.9 | 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":48107,"numValue":-3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48108,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48109,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7935,"numValue":9.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,291 | train | mutant | 5,951 | 117 | 6,521 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D165G | D165G | 1 | 1 | 0 | 0 | 165 | D | G | 9 | CONSERVATION | 1STN | 140 | null | 165 | A | L | true | true | 35.751861 | 13.31375 | 12,821 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D83G | null | null | 2.9 | 2.7 | null | null | null | 0.44 | 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 | 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":46621,"numValue":2.9,"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":46622,"numValue":2.7,"references":[],"strValue":null,"t... | [{"id":7935,"numValue":9.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,292 | train | mutant | 5,951 | 117 | 6,521 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D165G | D165G | 1 | 1 | 0 | 0 | 165 | D | G | 9 | CONSERVATION | 1STN | 140 | null | 165 | A | L | true | true | 35.751861 | 13.31375 | 13,142 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D83G | null | null | -2.8 | null | null | null | null | null | 0.93 | 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":48110,"numValue":-2.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48111,"numValue":0.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48112,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7935,"numValue":9.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,294 | train | mutant | 1,287 | 117 | 1,437 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166F | K166F | 1 | 1 | 0 | 0 | 166 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 2,451 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K84F | 49.2 | -3.5 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"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":9014,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9015,"numValue":-3.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9016,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9017,"numValue":null,"references":[],"... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,295 | train | mutant | 1,287 | 117 | 1,437 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166F | K166F | 1 | 1 | 0 | 0 | 166 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 2,546 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K84F | 50.6 | -2.4 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9394,"numValue":50.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9395,"numValue":-2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,296 | train | mutant | 1,287 | 117 | 1,437 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166F | K166F | 1 | 1 | 0 | 0 | 166 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 13,354 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K84F | null | null | 4.6 | 0.9 | null | null | null | 0.74 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49125,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49126,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49127,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49128,"numValue":0.74,... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,297 | train | mutant | 6,008 | 117 | 6,578 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166A | K166A | 1 | 1 | 0 | 0 | 166 | K | A | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 12,882 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K84A | null | null | 5.8 | -0.2 | null | null | null | 0.8 | 1.06 | 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":46926,"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":46927,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46928,"numValue":1.06,"reference... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,298 | train | mutant | 6,009 | 117 | 6,579 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166G | K166G | 1 | 1 | 0 | 0 | 166 | K | G | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 12,883 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K84G | null | null | 5.3 | 0.3 | null | null | null | 0.73 | 1.05 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46931,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46932,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46933,"numValue":1.05,"references... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,299 | train | mutant | 6,066 | 117 | 6,651 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166E | K166E | 1 | 1 | 0 | 0 | 166 | K | E | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 12,943 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K84E | null | null | 5.4 | 0 | null | null | null | 0.82 | 6.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47231,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47232,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47233,"numValue":6... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,300 | train | mutant | 6,067 | 117 | 6,652 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K166Q | K166Q | 1 | 1 | 0 | 0 | 166 | K | Q | 7 | CONSERVATION | 1STN | 140 | null | 166 | A | T | true | true | 172.844463 | 24.933334 | 12,944 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K84Q | null | null | 5.3 | 0.1 | null | null | null | 0.79 | 6.73 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47236,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47237,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47238,"numValue":6.73,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4723... | [{"id":7936,"numValue":7.0,"position":166,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,302 | train | mutant | 1,232 | 117 | 1,382 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167F | Y167F | 1 | 1 | 0 | 0 | 167 | Y | F | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 2,490 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y85F | 53.3 | 0.3 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":9170,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","guerios_625_map.csv","PoPMuSiC-2.0_S2648.csv","potapov_with_uniprot_mapping.csv","STRUM_Q3421.csv"],"id":9171,"numValue":0.3,"references":[],"strV... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,303 | train | mutant | 1,232 | 117 | 1,382 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167F | Y167F | 1 | 1 | 0 | 0 | 167 | Y | F | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 13,355 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y85F | null | null | 5.3 | 0.2 | null | null | null | 0.82 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":49130,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49131,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["g... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,304 | train | mutant | 1,232 | 117 | 1,382 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167F | Y167F | 1 | 1 | 0 | 0 | 167 | Y | F | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 13,498 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y85F | null | null | 5.6 | 0 | null | null | null | 0.83 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":49836,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49837,"numValue":0.0,"references":[],"strValue":null,"type":"DDG... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,305 | train | mutant | 1,238 | 117 | 1,388 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167L | Y167L | 1 | 1 | 0 | 0 | 167 | Y | L | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 2,401 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y85L | 52 | -0.7 | null | null | null | null | 90 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"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":["STRUM_Q3421.csv"],"id":8814,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":8815,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":8816,"numValue":90.0,"references":[],"strValue":null,"type... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,306 | train | mutant | 1,238 | 117 | 1,388 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167L | Y167L | 1 | 1 | 0 | 0 | 167 | Y | L | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 2,496 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y85L | 52.3 | -0.7 | 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":"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":9194,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9195,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9196,"numValue":85.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9197,"numValue":null,"references":[],"... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,307 | train | mutant | 1,238 | 117 | 1,388 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167L | Y167L | 1 | 1 | 0 | 0 | 167 | Y | L | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 13,505 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y85L | null | null | 5.5 | 0.1 | null | null | null | 0.8 | 1.02 | 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":49868,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49869,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49870,"numValue":1.02,"references... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,308 | train | mutant | 6,324 | 117 | 6,924 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167A | Y167A | 1 | 1 | 0 | 0 | 167 | Y | A | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 13,460 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y85A | null | null | 5.08 | 0.4 | null | null | null | 0.7 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49647,"numValue":5.08,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49648,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49649,"numValue":1.01,"reference... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,309 | train | mutant | 6,325 | 117 | 6,925 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y167G | Y167G | 1 | 1 | 0 | 0 | 167 | Y | G | 9 | CONSERVATION | 1STN | 140 | null | 167 | A | T | true | true | 157.547175 | 18.133333 | 13,461 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y85G | null | null | 4.48 | 1 | null | null | null | 0.6 | 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 | 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":49652,"numValue":4.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49653,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49654,"numValue":1.03,"references":[],"strValue":n... | [{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,311 | train | mutant | 1,288 | 117 | 1,438 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G168F | G168F | 1 | 1 | 0 | 0 | 168 | G | F | 6 | CONSERVATION | 1STN | 140 | null | 168 | A | S | false | false | 46.120662 | 11.6675 | 2,452 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:G86F | 43.6 | -9.1 | 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":"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":9018,"numValue":43.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9019,"numValue":-9.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9020,"numValue":72.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9021,"numValue":null,"references":[],"... | [{"id":7938,"numValue":6.0,"position":168,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,312 | train | mutant | 1,288 | 117 | 1,438 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G168F | G168F | 1 | 1 | 0 | 0 | 168 | G | F | 6 | CONSERVATION | 1STN | 140 | null | 168 | A | S | false | false | 46.120662 | 11.6675 | 2,547 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:G86F | 44.5 | -8.5 | null | null | null | null | 72 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9398,"numValue":44.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9399,"numValue":-8.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9400,"numValue":72.0,"references":[],"strV... | [{"id":7938,"numValue":6.0,"position":168,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,313 | train | mutant | 1,288 | 117 | 1,438 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G168F | G168F | 1 | 1 | 0 | 0 | 168 | G | F | 6 | CONSERVATION | 1STN | 140 | null | 168 | A | S | false | false | 46.120662 | 11.6675 | 13,356 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G86F | null | null | 3.5 | 2 | null | null | null | 0.53 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49135,"numValue":3.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49136,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49137,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49138,"numValue":0.53,... | [{"id":7938,"numValue":6.0,"position":168,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,315 | train | mutant | 6,134 | 117 | 6,722 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G168A | G168A | 1 | 1 | 0 | 0 | 168 | G | A | 6 | CONSERVATION | 1STN | 140 | null | 168 | A | S | false | false | 46.120662 | 11.6675 | 13,562 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G86A | null | null | 4.9 | 0.5 | null | null | null | 0.79 | 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":50140,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50141,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50142,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5014... | [{"id":7938,"numValue":6.0,"position":168,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7316 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,316 | train | mutant | 6,135 | 117 | 6,723 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G168V | G168V | 1 | 1 | 0 | 0 | 168 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 168 | A | S | false | false | 46.120662 | 11.6675 | 13,047 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G86V | null | null | 1.8 | 3.7 | null | null | null | 0.25 | 1.07 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47706,"numValue":1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47707,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47708,"numValue":1.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47709,"numValue":0.25,... | [{"id":7938,"numValue":6.0,"position":168,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,317 | train | mutant | 6,035 | 117 | 6,605 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R169A | R169A | 1 | 1 | 0 | 0 | 169 | R | A | 9 | ACTIVE_SITE|CONSERVATION | 1STN | 140 | null | 169 | A | L | true | true | 61.913372 | 13.658182 | 12,910 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R87A | null | null | 4.7 | 0.9 | null | null | null | 0.7 | 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 | 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":47066,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47067,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47068,"numValue":0.99,"references":[],"strValue":nu... | [{"id":33,"numValue":null,"position":169,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7939,"numValue":9.0,"position":169,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,318 | train | mutant | 6,036 | 117 | 6,606 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R169G | R169G | 1 | 1 | 0 | 0 | 169 | R | G | 9 | ACTIVE_SITE|CONSERVATION | 1STN | 140 | null | 169 | A | L | true | true | 61.913372 | 13.658182 | 12,911 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R87G | null | null | 3 | 2.6 | null | null | null | 0.44 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47071,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47072,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47073,"numValue":0.95,"references":[],"strValue":nu... | [{"id":33,"numValue":null,"position":169,"positionArray":null,"positionRange":null,"strValue":null,"type":"ACTIVE_SITE"},{"id":7939,"numValue":9.0,"position":169,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,319 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 216 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:G88V | 54.3 | 2.9 | null | null | 62 | 2.47 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":896,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":897,"numValue":2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":898,"numValue":62.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":899... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,321 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 3,035 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:G88V | 58.4 | 4.3 | null | null | 81.1 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv"],"id":11029,"numValue":58.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":11030,"numValue":4.3,"references":[],"strValue":null,"... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:7322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,322 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 3,036 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:G88V | 64.8 | null | null | null | 81.1 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv"],"id":11034,"numValue":64.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv"],"id":11035,"numValue":81.1,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:7323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,323 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 7,606 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | 51.4 | NaCl | 0.1 M | 1STN_A:G88V | null | null | null | -0.5 | null | 2.47 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_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 | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":51.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER... | [{"datasets":[],"id":26272,"numValue":2.47,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26273,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26274,"numValue":null,"referenc... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,324 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 7,793 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | 47 | NaCl | 0.1 M | 1STN_A:G88V | null | null | null | -0.6 | null | 2.47 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER... | [{"datasets":[],"id":26716,"numValue":2.47,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26717,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26718,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,325 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,049 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88V | null | null | 4.6 | 0.9 | null | null | null | 0.86 | 0.78 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47716,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47717,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47718,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4771... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,326 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,121 | ProTherm | 7 | Fluorescence | GdnHCl | Na3PO4 | 25 mM | 20 | NaCl | 0.1 M | 1STN_A:G88V | null | null | 4.6 | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 837 | ARTICLE | Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction. | 1,988 | 10.1021/bi00413a027 | 3167015 | Biochemistry;27;4761-8 | 3 | Freire E|Shortle D|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":"Na3PO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BU... | [{"datasets":[],"id":48047,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":48048,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48049,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,327 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,298 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88V | null | null | null | 0.9 | null | null | null | null | 0.78 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | 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":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":48860,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48861,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48862,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,328 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,313 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88V | null | null | 4.6 | 1 | null | null | null | 0.86 | 0.78 | 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 | 843 | ARTICLE | Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. | 1,986 | 10.1002/prot.340010113 | 3449854 | Proteins;1;81-9 | 2 | Shortle D|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":48921,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":48922,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48923,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48924,"numValue":0.86,... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7329 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,329 | train | mutant | 110 | 117 | 121 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170V | G170V | 1 | 1 | 0 | 0 | 170 | G | V | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,319 | ProTherm | 7 | Fluorescence | Urea | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88V | null | null | 5.2 | 0.9 | null | null | null | 2.72 | 0.85 | 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 | 843 | ARTICLE | Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. | 1,986 | 10.1002/prot.340010113 | 3449854 | Proteins;1;81-9 | 2 | Shortle D|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":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","t... | [{"datasets":[],"id":48951,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":48952,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48953,"numValue":0.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4895... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,330 | train | mutant | 1,596 | 117 | 1,796 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170W | G170W | 1 | 1 | 0 | 0 | 170 | G | W | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 2,991 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate,Sodium sulfate, | 10 mM,10 mM, | null | 1STN_A:G88W | 58.2 | 4.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|M47andM8_S1810.csv|Saraboji_S1791.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E 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,Sodium sulfate,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"},{"numValue":n... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":10858,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,331 | train | mutant | 1,596 | 117 | 1,796 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170W | G170W | 1 | 1 | 0 | 0 | 170 | G | W | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 3,011 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:G88W | 58.7 | 4.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|AUTOMUTE_S1962.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 268 | ARTICLE | Energetics of denaturation and m values of staphylococcal nuclease mutants. | 1,995 | 10.1021/bi00006a025 | 7849061 | Biochemistry;34;2034-41 | 2 | Privalov P L|Carra J H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10924,"numValue":58.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10925,"numValue":4.6,"references":[],"strValue":null,"type":"DTM"},{"data... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,332 | train | mutant | 1,596 | 117 | 1,796 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170W | G170W | 1 | 1 | 0 | 0 | 170 | G | W | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,307 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88W | null | null | 4.11 | 1.22 | null | null | null | 0.92 | 4.46 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E 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":48891,"numValue":4.11,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48892,"numValue":1.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48893,"numValue":4.46,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48894,"numValue":0.92,"references":[],... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,333 | train | mutant | 1,596 | 117 | 1,796 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170W | G170W | 1 | 1 | 0 | 0 | 170 | G | W | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,310 | ProTherm | 7 | CD | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88W | null | null | 4.33 | 0.69 | null | null | null | 0.95 | 4.6 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"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":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BU... | [{"datasets":[],"id":48906,"numValue":4.33,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48907,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48908,"numValue":4.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48909,"numValue":0.95,"references":[],"... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,334 | train | mutant | 6,136 | 117 | 6,724 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G170A | G170A | 1 | 1 | 0 | 0 | 170 | G | A | 6 | CONSERVATION | 1STN | 140 | null | 170 | A | E | true | false | 0.403113 | 8.6 | 13,048 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G88A | null | null | 5.4 | 0.1 | null | null | null | 0.87 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47711,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47712,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47713,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4771... | [{"id":7940,"numValue":6.0,"position":170,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,335 | train | mutant | 1,789 | 117 | 2,003 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L171F | L171F | 1 | 1 | 0 | 0 | 171 | L | F | 9 | CONSERVATION | 1STN | 140 | null | 171 | A | E | true | true | 26.462045 | 8.78875 | 3,441 | ProTherm | 5.38 | NMR | Thermal | Unknown | null | NaCl | 0.3 M | 1STN_A:L89F | 40.3 | -7.5 | null | null | null | null | 43.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.38,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.3 M","type":"ION_CONC"},{"numVa... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv"],"id":12716,"numValue":40.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["... | [{"id":7941,"numValue":9.0,"position":171,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,336 | train | mutant | 1,789 | 117 | 2,003 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L171F | L171F | 1 | 1 | 0 | 0 | 171 | L | F | 9 | CONSERVATION | 1STN | 140 | null | 171 | A | E | true | true | 26.462045 | 8.78875 | 8,090 | ProTherm | 5.38 | NMR | Thermal | Unknown | 40 | NaCl | 0.3 M | 1STN_A:L89F | null | null | 0.2 | 1.2 | null | 0 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.38,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":27504,"numValue":0.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27505,"numValue":0.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27506,"numValue":1.2,"references":... | [{"id":7941,"numValue":9.0,"position":171,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,338 | train | mutant | 5,924 | 117 | 6,494 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L171V | L171V | 1 | 1 | 0 | 0 | 171 | L | V | 9 | CONSERVATION | 1STN | 140 | null | 171 | A | E | true | true | 26.462045 | 8.78875 | 12,768 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L89V | null | null | 4 | 1.4 | null | null | null | 0.6 | 6.69 | 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":46367,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46368,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46369,"numValue":6.69,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46370,"numValue":0.6,"... | [{"id":7941,"numValue":9.0,"position":171,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,339 | train | mutant | 6,288 | 117 | 6,888 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L171A | L171A | 1 | 1 | 0 | 0 | 171 | L | A | 9 | CONSERVATION | 1STN | 140 | null | 171 | A | E | true | true | 26.462045 | 8.78875 | 13,415 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L89A | null | null | 2.88 | 2.6 | null | null | null | 0.4 | 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 | 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":49423,"numValue":2.88,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49424,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49425,"numValue":1.0,"references":[],"strValue":nu... | [{"id":7941,"numValue":9.0,"position":171,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,340 | train | mutant | 6,289 | 117 | 6,889 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L171G | L171G | 1 | 1 | 0 | 0 | 171 | L | G | 9 | CONSERVATION | 1STN | 140 | null | 171 | A | E | true | true | 26.462045 | 8.78875 | 13,416 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L89G | null | null | 2.28 | 3.2 | null | null | null | 0.3 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | 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":49428,"numValue":2.28,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49429,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49430,"numValue":0.96,"references":[],"strValue":n... | [{"id":7941,"numValue":9.0,"position":171,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,341 | train | mutant | 111 | 117 | 122 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172S | A172S | 1 | 1 | 0 | 0 | 172 | A | S | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 217 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:A90S | 40.7 | -10.7 | null | null | 92 | 2.43 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":901,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":902,"numValue":-10.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":903,"numValue":92.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":9... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,342 | train | mutant | 111 | 117 | 122 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172S | A172S | 1 | 1 | 0 | 0 | 172 | A | S | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 223 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:A90S | 33.5 | -13.5 | null | null | 65 | 2.43 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":931,"numValue":33.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":932,"numValue":-13.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":933,"numValue":65.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":9... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,343 | train | mutant | 111 | 117 | 122 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172S | A172S | 1 | 1 | 0 | 0 | 172 | A | S | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 7,607 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | 51.4 | NaCl | 0.1 M | 1STN_A:A90S | null | null | null | 2.5 | null | 2.43 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":51.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER... | [{"datasets":[],"id":26275,"numValue":2.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26276,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26277,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7344 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,344 | train | mutant | 111 | 117 | 122 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172S | A172S | 1 | 1 | 0 | 0 | 172 | A | S | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 7,794 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | 47 | NaCl | 0.1 M | 1STN_A:A90S | null | null | null | 2.6 | null | 2.43 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER... | [{"datasets":[],"id":26719,"numValue":2.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26720,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26721,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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