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:7573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,573 | train | mutant | 1,274 | 117 | 1,424 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T202I | T202I | 1 | 1 | 0 | 0 | 202 | T | I | 7 | CONSERVATION | 1STN | 140 | null | 202 | A | T | false | false | 51.30751 | 17.551429 | 12,784 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T120I | null | null | 3.7 | 1.7 | null | null | null | 0.61 | 5.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46447,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46448,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46449,"numValue":5.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46450,"numValue":0.61,... | [{"id":7972,"numValue":7.0,"position":202,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,574 | train | mutant | 6,179 | 117 | 6,767 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T202G | T202G | 1 | 1 | 0 | 0 | 202 | T | G | 7 | CONSERVATION | 1STN | 140 | null | 202 | A | T | false | false | 51.30751 | 17.551429 | 13,097 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T120G | null | null | 3.4 | 2.1 | null | null | null | 0.56 | 0.9 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47954,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47955,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47956,"numValue":0.9,"references":[],"strValue":nul... | [{"id":7972,"numValue":7.0,"position":202,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,575 | train | mutant | 6,180 | 117 | 6,768 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | T202A | T202A | 1 | 1 | 0 | 0 | 202 | T | A | 7 | CONSERVATION | 1STN | 140 | null | 202 | A | T | false | false | 51.30751 | 17.551429 | 13,098 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:T120A | null | null | 4.3 | 1.2 | null | null | null | 0.66 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47959,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47960,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47961,"numValue":0.94,"references":[],"strValue":nu... | [{"id":7972,"numValue":7.0,"position":202,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,576 | train | mutant | 6,027 | 117 | 6,597 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H203A | H203A | 1 | 1 | 0 | 0 | 203 | H | A | 7 | CONSERVATION | 1STN | 140 | null | 203 | A | T | false | false | 39.028952 | 15.113 | 12,902 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:H121A | null | null | 2.5 | 3.1 | null | null | null | 0.4 | 0.87 | 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":47026,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47027,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47028,"numValue":0.87,"references":[],"strValue":nu... | [{"id":7973,"numValue":7.0,"position":203,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,577 | train | mutant | 6,028 | 117 | 6,598 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H203G | H203G | 1 | 1 | 0 | 0 | 203 | H | G | 7 | CONSERVATION | 1STN | 140 | null | 203 | A | T | false | false | 39.028952 | 15.113 | 12,903 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:H121G | null | null | 1.4 | 4.2 | null | null | null | 0.22 | 0.83 | 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":47031,"numValue":1.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47032,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47033,"numValue":0.83,"references":[],"strValue":nu... | [{"id":7973,"numValue":7.0,"position":203,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,578 | train | mutant | 1,293 | 117 | 1,443 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204F | E204F | 1 | 1 | 0 | 0 | 204 | E | F | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 2,457 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E122F | 51.7 | -1 | null | null | null | null | 91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|HotMuSiC_S1626.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1962.csv","HotMuSiC_S1626.csv","Saraboji_S2204.csv"],"id":9038,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","HotMuSiC_S1626.csv","Saraboji_S2204.csv"],"id":9039,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,579 | train | mutant | 1,293 | 117 | 1,443 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204F | E204F | 1 | 1 | 0 | 0 | 204 | E | F | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 2,552 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E122F | 52.8 | -0.2 | 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":"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":9418,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9419,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9420,"numValue":80.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9421,"numValue":null,"references":[],"... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,580 | train | mutant | 1,293 | 117 | 1,443 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204F | E204F | 1 | 1 | 0 | 0 | 204 | E | F | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 13,368 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E122F | null | null | 4.7 | 0.8 | null | null | null | 0.82 | 0.86 | 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":49195,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49196,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49197,"numValue":0.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49198,"numValue":0.82,... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,581 | train | mutant | 5,971 | 117 | 6,541 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204A | E204A | 1 | 1 | 0 | 0 | 204 | E | A | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 12,844 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E122A | null | null | 5.2 | 0.4 | null | null | null | 0.78 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46736,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46737,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46738,"numValue":0.97,"references... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,582 | train | mutant | 5,972 | 117 | 6,542 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204G | E204G | 1 | 1 | 0 | 0 | 204 | E | G | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 12,845 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E122G | null | null | 3.4 | 2.2 | null | null | null | 0.54 | 0.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46741,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46742,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46743,"numValue":0.89,"references":[],"strValue":nu... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,583 | train | mutant | 6,070 | 117 | 6,655 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204K | E204K | 1 | 1 | 0 | 0 | 204 | E | K | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 12,947 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E122K | null | null | 2.7 | 2.7 | null | null | null | 0.46 | 5.87 | 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 | 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":47251,"numValue":2.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47252,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47253,"numValue":5.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47254,"numValue":0.46,... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,584 | train | mutant | 6,071 | 117 | 6,656 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E204Q | E204Q | 1 | 1 | 0 | 0 | 204 | E | Q | 6 | CONSERVATION | 1STN | 140 | null | 204 | A | H | true | false | 32.961892 | 21.238889 | 12,948 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E122Q | null | null | 3.8 | 1.6 | null | null | null | 0.6 | 6.2 | 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":47256,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47257,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47258,"numValue":6.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47259,"numValue":0.6,"r... | [{"id":7974,"numValue":6.0,"position":204,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,586 | train | mutant | 1,294 | 117 | 1,444 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q205F | Q205F | 1 | 1 | 0 | 0 | 205 | Q | F | 5 | CONSERVATION | 1STN | 140 | null | 205 | A | H | false | false | 112.735708 | 33.985556 | 2,553 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Q123F | 52.5 | -0.5 | null | null | null | null | 86 | 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":9422,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9423,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9424,"numValue":86.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9425,"numValue":null,"references":[],"... | [{"id":7975,"numValue":5.0,"position":205,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,587 | train | mutant | 1,294 | 117 | 1,444 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q205F | Q205F | 1 | 1 | 0 | 0 | 205 | Q | F | 5 | CONSERVATION | 1STN | 140 | null | 205 | A | H | false | false | 112.735708 | 33.985556 | 13,369 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q123F | null | null | 4.8 | 0.7 | null | null | null | 0.78 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49200,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49201,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49202,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49203,"numValue":0.78,... | [{"id":7975,"numValue":5.0,"position":205,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,589 | train | mutant | 6,158 | 117 | 6,746 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q205A | Q205A | 1 | 1 | 0 | 0 | 205 | Q | A | 5 | CONSERVATION | 1STN | 140 | null | 205 | A | H | false | false | 112.735708 | 33.985556 | 13,071 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q123A | null | null | 5.1 | 0.4 | null | null | null | 0.83 | 0.9 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|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":47824,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47825,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47826,"numValue":0.9,"references"... | [{"id":7975,"numValue":5.0,"position":205,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,590 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 218 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:H124L | 56.5 | 5.1 | null | null | 81 | 2 | 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":906,"numValue":56.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":907,"numValue":5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":908,"numValue":81.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":909... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,591 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 224 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 1STN_A:H124L | 55.3 | 8.3 | null | null | 56 | 2 | 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":936,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":937,"numValue":8.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":938,"numValue":56.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":939... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,592 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,423 | ProTherm | 7 | Fluorescence | Thermal | Tris-HCl | 0.01 M | null | NaCl | 0.1 M | 1STN_A:H124L | 56.4 | 5.8 | null | null | null | null | 92 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|STRUM_Q306.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 304 | ARTICLE | Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids. | 1,991 | 10.1021/bi00219a005 | 1991099 | Biochemistry;30;1193-9 | 4 | Eftink M R|Ghiron C A|Kautz R A|Fox R O | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["AUTOMUTE_S1962.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":12630,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":12631,"numValue":5.8,"references":[],"strValue":null,"type":"DTM"},{"datas... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,593 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,445 | ProTherm | 5.2 | NMR | Thermal | Unknown | null | NaCl | 0.3 M | 1STN_A:H124L | 56.2 | 8.4 | null | null | null | null | 86.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.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":5.2,"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"},{"numVal... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12732,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":12733,"numValue":8.4,"references":[],"strValue":null,... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,594 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,547 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 56 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13067,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13068,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,595 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,548 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 58 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13069,"numValue":58.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13070,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,596 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,549 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 51.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13071,"numValue":51.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13072,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,597 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,550 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 64.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13073,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13074,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,598 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,551 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 49 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13075,"numValue":49.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13076,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,599 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,552 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 54 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13077,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13078,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,600 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 3,553 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | null | 1STN_A:H124L | 30 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|Broom_S605.csv | 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:H124L","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13079,"numValue":30.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv"],"id":13080,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,601 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 7,608 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | 51.4 | NaCl | 0.1 M | 1STN_A:H124L | null | null | null | -1.3 | null | 2 | 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":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":26278,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26279,"numValue":-1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26280,"numValue":null,"references":[],"strValue":"yes","type":"R... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,602 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 7,795 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | 47 | NaCl | 0.1 M | 1STN_A:H124L | null | null | null | -1.9 | null | 2 | 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":26722,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26723,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26724,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,603 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 8,084 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | 40 | 1STN_A:H124L | null | null | 4.39 | null | null | null | 90.3 | 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":27486,"numValue":90.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":27487,"numValue":4.39,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":27488,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,605 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 8,086 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | 40 | 1STN_A:H124L | null | null | 1.83 | null | null | null | 52.8 | 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":27492,"numValue":52.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":27493,"numValue":1.83,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":27494,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,606 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 8,087 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | 40 | 1STN_A:H124L | null | null | 5.85 | null | null | null | 80.9 | 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":27495,"numValue":80.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":27496,"numValue":5.85,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":27497,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,607 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 8,088 | ProTherm | 5.5 | NMR | Thermal | Bis-Tris | 10 mM | 40 | 1STN_A:H124L | null | null | 1.92 | null | null | null | 69 | 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":27498,"numValue":69.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":27499,"numValue":1.92,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":27500,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,609 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 8,093 | ProTherm | 5.2 | NMR | Thermal | Unknown | 40 | NaCl | 0.3 M | 1STN_A:H124L | null | null | 2.1 | -0.7 | null | 0 | 1 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.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":5.2,"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"},{"nu... | [{"datasets":[],"id":27516,"numValue":0.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27517,"numValue":1.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":27518,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,611 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,663 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21.5 | 1STN_A:H124L | null | null | 4.98 | null | null | null | null | 1.05 | 8.08 | 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":45912,"numValue":4.98,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45913,"numValue":8.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45914,"numValue":1.05,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45915,"numValue":null,"references":[],"... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,612 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,664 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21.5 | 1STN_A:H124L | null | null | 5.39 | null | null | null | null | 1.06 | 8.65 | 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":45916,"numValue":5.39,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45917,"numValue":8.65,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45918,"numValue":1.06,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45919,"numValue":null,"references":[],"... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,613 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,665 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21.5 | 1STN_A:H124L | null | null | 5.55 | null | null | null | null | 1.08 | 8.76 | 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":45920,"numValue":5.55,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45921,"numValue":8.76,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45922,"numValue":1.08,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45923,"numValue":null,"references":[],"... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,615 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,667 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21.5 | 1STN_A:H124L | null | null | 5.95 | null | null | null | null | 1.23 | 8.25 | 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":45928,"numValue":5.95,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45929,"numValue":8.25,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45930,"numValue":1.23,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45931,"numValue":null,"references":[],"... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,616 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,668 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21.5 | 1STN_A:H124L | null | null | 2.76 | null | null | null | null | 0.52 | 9.04 | 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":45932,"numValue":2.76,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45933,"numValue":9.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45934,"numValue":0.52,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45935,"numValue":null,"references":[],"... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,617 | train | mutant | 112 | 117 | 123 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206L | H206L | 1 | 1 | 0 | 0 | 206 | H | L | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,701 | ProTherm | 5.5 | Fluorescence | GdnHCl | Bis-Tris | 10 mM | 21 | 1STN_A:H124L | null | null | 1.9 | null | null | null | null | 0.75 | 5.8 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 816 | ARTICLE | High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. | 1,996 | 10.1021/bi952012g | 8620010 | Biochemistry;35;3857-64 | 4 | Markley J L|Truckses D M|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":21.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"... | [{"datasets":[],"id":46064,"numValue":1.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46065,"numValue":5.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46066,"numValue":0.75,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":46067,"numValue":null,"references":[],"st... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,618 | train | mutant | 6,029 | 117 | 6,599 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206A | H206A | 1 | 1 | 0 | 0 | 206 | H | A | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,904 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:H124A | null | null | 6 | -0.4 | null | null | null | 0.91 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47036,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47037,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47038,"numValue":0.96,"reference... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,620 | train | mutant | 6,072 | 117 | 6,657 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206E | H206E | 1 | 1 | 0 | 0 | 206 | H | E | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,949 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:H124E | null | null | 5.6 | -0.2 | null | null | null | 0.93 | 6.07 | 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":47261,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47262,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47263,"numValue":6.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":472... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,621 | train | mutant | 6,073 | 117 | 6,658 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206Q | H206Q | 1 | 1 | 0 | 0 | 206 | H | Q | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 12,950 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:H124Q | null | null | 6 | -0.6 | null | null | null | 0.94 | 6.4 | 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":47266,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47267,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47268,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4726... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,622 | train | mutant | 6,256 | 117 | 6,851 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | H206F | H206F | 1 | 1 | 0 | 0 | 206 | H | F | 4 | CONSERVATION | 1STN | 140 | null | 206 | A | H | false | false | 95.045475 | 25.575 | 13,370 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:H124F | null | null | 5.8 | -0.3 | null | null | null | 0.94 | 0.93 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49205,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49206,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49207,"numValue":0.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":492... | [{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,623 | train | mutant | 5,929 | 117 | 6,499 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207I | L207I | 1 | 1 | 0 | 0 | 207 | L | I | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 12,773 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L125I | null | null | 4.4 | 1 | null | null | null | 0.68 | 6.54 | 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":46392,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46393,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46394,"numValue":6.54,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46395,"numValue":0.68,... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,624 | train | mutant | 5,930 | 117 | 6,500 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207V | L207V | 1 | 1 | 0 | 0 | 207 | L | V | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 12,774 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L125V | null | null | 3.1 | 2.3 | null | null | null | 0.47 | 6.57 | 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":46397,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46398,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46399,"numValue":6.57,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46400,"numValue":0.47,... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,625 | train | mutant | 6,223 | 117 | 6,817 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207E | L207E | 1 | 1 | 0 | 0 | 207 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 13,268 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L125E | null | null | 5.5 | 4 | null | null | null | 1.2 | 4.8 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":3.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48722,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48723,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48724,"numValue":4.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48725,"numValue":1.2,"references":[],"str... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,626 | train | mutant | 6,223 | 117 | 6,817 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207E | L207E | 1 | 1 | 0 | 0 | 207 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 13,269 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L125E | null | null | 7.2 | 4.6 | null | null | null | 1.4 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48727,"numValue":7.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48728,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48729,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48730,"numValue":1.4,"references":[],"str... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,627 | train | mutant | 6,223 | 117 | 6,817 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207E | L207E | 1 | 1 | 0 | 0 | 207 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 13,270 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L125E | null | null | 5.9 | 5.8 | null | null | null | 1.1 | 5.4 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48732,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48733,"numValue":5.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48734,"numValue":5.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48735,"numValue":1.1,"references":[],"str... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,628 | train | mutant | 6,223 | 117 | 6,817 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207E | L207E | 1 | 1 | 0 | 0 | 207 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 13,271 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L125E | null | null | 3.7 | 8.2 | null | null | null | 0.7 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":7.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48737,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48738,"numValue":8.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48739,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48740,"numValue":0.7,"references":[],"str... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,629 | train | mutant | 6,223 | 117 | 6,817 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207E | L207E | 1 | 1 | 0 | 0 | 207 | L | E | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 13,272 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L125E | null | null | 2.5 | 9.1 | null | null | null | 0.5 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48742,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48743,"numValue":9.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48744,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48745,"numValue":0.5,"references":[],"str... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,630 | train | mutant | 6,290 | 117 | 6,890 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L207A | L207A | 1 | 1 | 0 | 0 | 207 | L | A | 7 | CONSERVATION | 1STN | 140 | null | 207 | A | H | true | false | 0 | 16.63 | 13,418 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L125A | null | null | 0.38 | 4.9 | null | null | null | 0.1 | 0.66 | 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":49438,"numValue":0.38,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49439,"numValue":4.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49440,"numValue":0.66,"references":[],"strValue":n... | [{"id":7977,"numValue":7.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,631 | train | mutant | 6,039 | 117 | 6,609 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | R208A | R208A | 1 | 1 | 0 | 0 | 208 | R | A | 4 | CONSERVATION | 1STN | 140 | null | 208 | A | H | false | false | 93.381959 | 20.957273 | 12,914 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:R126A | null | null | 3.9 | 1.7 | null | null | null | 0.57 | 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 | 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":47086,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47087,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47088,"numValue":0.98,"references":[],"strValue":nu... | [{"id":7978,"numValue":4.0,"position":208,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,633 | train | mutant | 1,295 | 117 | 1,445 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209F | K209F | 1 | 1 | 0 | 0 | 209 | K | F | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 2,459 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K127F | 51.5 | -1.2 | null | null | null | null | 86 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":9046,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9047,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9048,"numValue":86.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"i... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,634 | train | mutant | 1,295 | 117 | 1,445 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209F | K209F | 1 | 1 | 0 | 0 | 209 | K | F | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 2,554 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K127F | 52.4 | -0.6 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv|AUTOMUTE_S1962.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":9426,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,635 | train | mutant | 1,295 | 117 | 1,445 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209F | K209F | 1 | 1 | 0 | 0 | 209 | K | F | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 13,371 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K127F | null | null | 5.2 | 0.3 | null | null | null | 0.81 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49210,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49211,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49212,"numValue":0.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4921... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,636 | train | mutant | 6,015 | 117 | 6,585 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209A | K209A | 1 | 1 | 0 | 0 | 209 | K | A | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 12,890 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K127A | null | null | 5.8 | -0.2 | null | null | null | 0.84 | 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 | 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":46966,"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":46967,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46968,"numValue":1.02,"reference... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,637 | train | mutant | 6,016 | 117 | 6,586 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209G | K209G | 1 | 1 | 0 | 0 | 209 | K | G | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 12,891 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K127G | null | null | 4.9 | 0.7 | null | null | null | 0.67 | 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 | 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":46971,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46972,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46973,"numValue":1.05,"references":[],"strValue":nu... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,638 | train | mutant | 6,074 | 117 | 6,659 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209E | K209E | 1 | 1 | 0 | 0 | 209 | K | E | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 12,951 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K127E | null | null | 5.4 | 0 | null | null | null | 0.86 | 6.34 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47271,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47272,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47273,"numValue":6... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,639 | train | mutant | 6,075 | 117 | 6,660 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K209Q | K209Q | 1 | 1 | 0 | 0 | 209 | K | Q | 4 | CONSERVATION | 1STN | 140 | null | 209 | A | H | false | false | 138.202066 | 28.325556 | 12,952 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K127Q | null | null | 5.4 | 0 | null | null | null | 0.84 | 6.4 | 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":47276,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47277,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47278,"numValue":6... | [{"id":7979,"numValue":4.0,"position":209,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,640 | train | mutant | 1,242 | 117 | 1,392 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210A | S210A | 1 | 1 | 0 | 0 | 210 | S | A | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 2,405 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:S128A | 55.7 | 3 | null | null | null | null | 94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | 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":["HotMuSiC_S1626.csv"],"id":8830,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":8831,"numValue":3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":8832,"numValue":94.0,"references":[],"strValue":null,"type":"DHVH"}... | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,641 | train | mutant | 1,242 | 117 | 1,392 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210A | S210A | 1 | 1 | 0 | 0 | 210 | S | A | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 2,500 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:S128A | 57.9 | 4.9 | null | null | null | null | 97 | 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":9210,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9211,"numValue":4.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9212,"numValue":97.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9213,"numValue":null,"references":[],"s... | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,642 | train | mutant | 1,242 | 117 | 1,392 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210A | S210A | 1 | 1 | 0 | 0 | 210 | S | A | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 4,339 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:S128A | 57.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 415 | ARTICLE | Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability. | 2,000 | 10.1006/jmbi.2000.4140 | 11023780 | J Mol Biol;303;125-30 | 4 | Chen J|Lu Z|Sakon J|Stites W E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":16063,"numValue":57.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":16064,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,643 | train | mutant | 1,242 | 117 | 1,392 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210A | S210A | 1 | 1 | 0 | 0 | 210 | S | A | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 13,078 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:S128A | null | null | 6.2 | -0.7 | null | null | null | 0.96 | 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 | 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":47859,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47860,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47861,"numValue":0.96,"references":[],"strValue":n... | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7644 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,644 | train | mutant | 1,242 | 117 | 1,392 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210A | S210A | 1 | 1 | 0 | 0 | 210 | S | A | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 13,624 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:S128A | null | null | 6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 415 | ARTICLE | Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability. | 2,000 | 10.1006/jmbi.2000.4140 | 11023780 | J Mol Biol;303;125-30 | 4 | Chen J|Lu Z|Sakon J|Stites W E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50403,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":50404,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,645 | train | mutant | 1,296 | 117 | 1,446 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210F | S210F | 1 | 1 | 0 | 0 | 210 | S | F | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 2,460 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:S128F | 48.9 | -3.8 | null | null | null | null | 81 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":9050,"numValue":48.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":9051,"numValue":-3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.... | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,647 | train | mutant | 1,296 | 117 | 1,446 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210F | S210F | 1 | 1 | 0 | 0 | 210 | S | F | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 13,372 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:S128F | null | null | 4.5 | 1 | null | null | null | 0.68 | 1 | 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":49215,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49216,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49217,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49218,"numValue":0.68,"... | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,648 | train | mutant | 6,163 | 117 | 6,751 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S210G | S210G | 1 | 1 | 0 | 0 | 210 | S | G | 6 | CONSERVATION | 1STN | 140 | null | 210 | A | H | false | false | 11.429817 | 13.89 | 13,077 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:S128G | null | null | 3.9 | 1.6 | null | null | null | 0.59 | 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 | 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":47854,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47855,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47856,"numValue":0.99,"references":[],"strValue":nu... | [{"id":7980,"numValue":6.0,"position":210,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7649 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,649 | train | mutant | 5,973 | 117 | 6,543 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E211A | E211A | 1 | 1 | 0 | 0 | 211 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 211 | A | H | false | false | 16.740155 | 15.434444 | 12,846 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E129A | null | null | 3.2 | 2.4 | null | null | null | 0.51 | 0.86 | 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":46746,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46747,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46748,"numValue":0.86,"references":[],"strValue":nu... | [{"id":7981,"numValue":8.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7650 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,650 | train | mutant | 5,974 | 117 | 6,544 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E211G | E211G | 1 | 1 | 0 | 0 | 211 | E | G | 8 | CONSERVATION | 1STN | 140 | null | 211 | A | H | false | false | 16.740155 | 15.434444 | 12,847 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E129G | null | null | 1.8 | 3.8 | null | null | null | 0.27 | 0.85 | 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":46751,"numValue":1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46752,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46753,"numValue":0.85,"references":[],"strValue":nu... | [{"id":7981,"numValue":8.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,651 | train | mutant | 6,257 | 117 | 6,852 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E211F | E211F | 1 | 1 | 0 | 0 | 211 | E | F | 8 | CONSERVATION | 1STN | 140 | null | 211 | A | H | false | false | 16.740155 | 15.434444 | 13,373 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E129F | null | null | 1.5 | 4 | null | null | null | 0.26 | 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 | 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":49220,"numValue":1.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49221,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49222,"numValue":0.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49223,"numValue":0.26,... | [{"id":7981,"numValue":8.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7652 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,652 | train | mutant | 6,107 | 117 | 6,695 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A212G | A212G | 1 | 1 | 0 | 0 | 212 | A | G | 4 | CONSERVATION | 1STN | 140 | null | 212 | A | H | false | false | 57.000908 | 13.848 | 13,018 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A130G | null | null | 4.4 | 1.1 | null | null | null | 0.67 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | 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":47561,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47562,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47563,"numValue":0.96,"references":[],"strValue":nu... | [{"id":7982,"numValue":4.0,"position":212,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,654 | train | mutant | 6,159 | 117 | 6,747 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q213G | Q213G | 1 | 1 | 0 | 0 | 213 | Q | G | 4 | CONSERVATION | 1STN | 140 | null | 213 | A | H | false | false | 61.37783 | 19.462222 | 13,072 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q131G | null | null | 3.1 | 2.4 | null | null | null | 0.49 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47829,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47830,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47831,"numValue":0.92,"references":[],"strValue":nu... | [{"id":7983,"numValue":4.0,"position":213,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,655 | train | mutant | 6,160 | 117 | 6,748 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q213A | Q213A | 1 | 1 | 0 | 0 | 213 | Q | A | 4 | CONSERVATION | 1STN | 140 | null | 213 | A | H | false | false | 61.37783 | 19.462222 | 13,073 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q131A | null | null | 5.3 | 0.2 | null | null | null | 0.8 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47834,"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":47835,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47836,"numValue":0.98,"references... | [{"id":7983,"numValue":4.0,"position":213,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,656 | train | mutant | 6,258 | 117 | 6,853 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q213F | Q213F | 1 | 1 | 0 | 0 | 213 | Q | F | 4 | CONSERVATION | 1STN | 140 | null | 213 | A | H | false | false | 61.37783 | 19.462222 | 13,374 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Q131F | null | null | 4.8 | 0.7 | null | null | null | 0.77 | 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":49225,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49226,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49227,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49228,"numValue":0.77,... | [{"id":7983,"numValue":4.0,"position":213,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,657 | train | mutant | 6,109 | 117 | 6,697 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A214G | A214G | 1 | 1 | 0 | 0 | 214 | A | G | 9 | CONSERVATION | 1STN | 140 | null | 214 | A | H | false | false | 0 | 15.606 | 13,020 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A132G | null | null | 1.8 | 3.7 | null | null | null | 0.29 | 0.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47571,"numValue":1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47572,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47573,"numValue":0.89,"references":[],"strValue":nu... | [{"id":7984,"numValue":9.0,"position":214,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,658 | train | mutant | 6,110 | 117 | 6,698 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A214V | A214V | 1 | 1 | 0 | 0 | 214 | A | V | 9 | CONSERVATION | 1STN | 140 | null | 214 | A | H | false | false | 0 | 15.606 | 13,021 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A132V | null | null | 0.7 | 4.8 | null | null | null | 0.12 | 0.86 | 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":47576,"numValue":0.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47577,"numValue":4.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47578,"numValue":0.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47579,"numValue":0.12,... | [{"id":7984,"numValue":9.0,"position":214,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,659 | train | mutant | 6,224 | 117 | 6,818 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A214E | A214E | 1 | 1 | 0 | 0 | 214 | A | E | 9 | CONSERVATION | 1STN | 140 | null | 214 | A | H | false | false | 0 | 15.606 | 13,273 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A132E | null | null | 6 | 5.8 | null | null | null | 1.2 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":4.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48747,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48748,"numValue":5.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48749,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48750,"numValue":1.2,"references":[],"str... | [{"id":7984,"numValue":9.0,"position":214,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,660 | train | mutant | 6,224 | 117 | 6,818 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A214E | A214E | 1 | 1 | 0 | 0 | 214 | A | E | 9 | CONSERVATION | 1STN | 140 | null | 214 | A | H | false | false | 0 | 15.606 | 13,274 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A132E | null | null | 4.9 | 6.8 | null | null | null | 0.9 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48752,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48753,"numValue":6.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48754,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48755,"numValue":0.9,"references":[],"str... | [{"id":7984,"numValue":9.0,"position":214,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,662 | train | mutant | 6,224 | 117 | 6,818 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A214E | A214E | 1 | 1 | 0 | 0 | 214 | A | E | 9 | CONSERVATION | 1STN | 140 | null | 214 | A | H | false | false | 0 | 15.606 | 13,276 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A132E | null | null | 3 | 8.5 | null | null | null | 0.8 | 3.9 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48762,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48763,"numValue":8.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48764,"numValue":3.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48765,"numValue":0.8,"references":[],"str... | [{"id":7984,"numValue":9.0,"position":214,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,664 | train | mutant | 6,018 | 117 | 6,588 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K215G | K215G | 1 | 1 | 0 | 0 | 215 | K | G | 7 | CONSERVATION | 1STN | 140 | null | 215 | A | H | false | false | 86.413175 | 30.232223 | 12,893 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K133G | null | null | 2.3 | 3.3 | null | null | null | 0.34 | 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":46981,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46982,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46983,"numValue":0.92,"references":[],"strValue":nu... | [{"id":7985,"numValue":7.0,"position":215,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,665 | train | mutant | 6,076 | 117 | 6,661 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K215Q | K215Q | 1 | 1 | 0 | 0 | 215 | K | Q | 7 | CONSERVATION | 1STN | 140 | null | 215 | A | H | false | false | 86.413175 | 30.232223 | 12,953 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K133Q | null | null | 4.9 | 0.5 | null | null | null | 0.76 | 6.53 | 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":47281,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47282,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47283,"numValue":6.53,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4728... | [{"id":7985,"numValue":7.0,"position":215,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7666 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,666 | train | mutant | 6,259 | 117 | 6,854 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K215F | K215F | 1 | 1 | 0 | 0 | 215 | K | F | 7 | CONSERVATION | 1STN | 140 | null | 215 | A | H | false | false | 86.413175 | 30.232223 | 13,375 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K133F | null | null | 4.1 | 1.4 | null | null | null | 0.66 | 0.93 | 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":49230,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49231,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49232,"numValue":0.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49233,"numValue":0.66,... | [{"id":7985,"numValue":7.0,"position":215,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7667 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,667 | train | mutant | 2,168 | 117 | 2,462 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216C | K216C | 1 | 1 | 0 | 0 | 216 | K | C | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 4,261 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K134C | 50.1 | -2.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":15797,"numValue":50.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15798,"numValue":-2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15799,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,668 | train | mutant | 2,168 | 117 | 2,462 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216C | K216C | 1 | 1 | 0 | 0 | 216 | K | C | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 13,610 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K134C | null | null | 4.8 | 0.7 | null | null | null | 0.73 | 6.57 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50348,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50349,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50350,"numValue":6.57,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50351,"numValue":0.73,... | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,669 | train | mutant | 2,173 | 117 | 2,467 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216F | K216F | 1 | 1 | 0 | 0 | 216 | K | F | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 4,269 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K134F | 51.3 | -1.7 | 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":15821,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15822,"numValue":-1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15823,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,670 | train | mutant | 2,173 | 117 | 2,467 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216F | K216F | 1 | 1 | 0 | 0 | 216 | K | F | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 13,376 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K134F | null | null | 5 | 0.5 | null | null | null | 0.82 | 0.93 | 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":49235,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49236,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49237,"numValue":0.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49238,"numValue":0.82,... | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,671 | train | mutant | 2,173 | 117 | 2,467 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216F | K216F | 1 | 1 | 0 | 0 | 216 | K | F | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 13,618 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K134F | null | null | 5.2 | 0.3 | null | null | null | 0.81 | 6.39 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":50388,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":50389,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50390,"numValue":6.39,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50391,"numValue":0.81,"... | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7672 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,672 | train | mutant | 6,019 | 117 | 6,589 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216A | K216A | 1 | 1 | 0 | 0 | 216 | K | A | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 12,894 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K134A | null | null | 5.7 | -0.1 | null | null | null | 0.82 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46986,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46987,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46988,"numValue":1.01,"reference... | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,673 | train | mutant | 6,020 | 117 | 6,590 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K216G | K216G | 1 | 1 | 0 | 0 | 216 | K | G | 3 | CONSERVATION | 1STN | 140 | null | 216 | A | H | false | false | 147.769997 | 35.506667 | 12,895 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K134G | null | null | 4.9 | 0.7 | null | null | null | 0.67 | 1.04 | 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":46991,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46992,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46993,"numValue":1.04,"references":[],"strValue":nu... | [{"id":7986,"numValue":3.0,"position":216,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,674 | train | mutant | 1,297 | 117 | 1,447 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217F | E217F | 1 | 1 | 0 | 0 | 217 | E | F | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 2,461 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E135F | 49.2 | -3.5 | null | null | null | null | 81 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | 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":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":9054,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":9055,"numValue":-3.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,675 | train | mutant | 1,297 | 117 | 1,447 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217F | E217F | 1 | 1 | 0 | 0 | 217 | E | F | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 2,556 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E135F | 49.5 | -3.5 | null | null | null | null | 76 | null | null | null | null | null | null | null | null | null | Unknown | 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_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|M47andM8_S1810.csv|PoPMuSiC-2.0_S2648.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":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv"],"id":9434,"numValue":49.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_M... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,676 | train | mutant | 1,297 | 117 | 1,447 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217F | E217F | 1 | 1 | 0 | 0 | 217 | E | F | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 13,377 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E135F | null | null | 4.3 | 1.2 | null | null | null | 0.68 | 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":49240,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49241,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49242,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49243,"numValue":0.68,... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,677 | train | mutant | 5,975 | 117 | 6,545 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217A | E217A | 1 | 1 | 0 | 0 | 217 | E | A | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 12,848 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E135A | null | null | 4.9 | 0.7 | null | null | null | 0.69 | 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":46756,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46757,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46758,"numValue":1.02,"references":[],"strValue":nu... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,678 | train | mutant | 5,976 | 117 | 6,546 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217G | E217G | 1 | 1 | 0 | 0 | 217 | E | G | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 12,849 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E135G | null | null | 3.9 | 1.7 | null | null | null | 0.57 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46761,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46762,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46763,"numValue":0.97,"references":[],"strValue":nu... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,679 | train | mutant | 6,077 | 117 | 6,662 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217K | E217K | 1 | 1 | 0 | 0 | 217 | E | K | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 12,954 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E135K | null | null | 4.3 | 1.1 | null | null | null | 0.63 | 6.8 | 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":47286,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47287,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47288,"numValue":6.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47289,"numValue":0.63,"... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,680 | train | mutant | 6,078 | 117 | 6,663 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E217Q | E217Q | 1 | 1 | 0 | 0 | 217 | E | Q | 3 | CONSERVATION | 1STN | 140 | null | 217 | A | T | false | false | 78.138302 | 16.931111 | 12,955 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E135Q | null | null | 4.7 | 0.7 | null | null | null | 0.71 | 6.6 | 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":47291,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47292,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47293,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47294,"numValue":0.71,"... | [{"id":7987,"numValue":3.0,"position":217,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,681 | train | mutant | 1,298 | 117 | 1,448 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K218F | K218F | 1 | 1 | 0 | 0 | 218 | K | F | 4 | CONSERVATION | 1STN | 140 | null | 218 | A | T | false | false | 140.289445 | 34.795556 | 2,462 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K136F | 46.3 | -6.4 | null | null | null | null | 74 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"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":9058,"numValue":46.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9059,"numValue":-6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9060,"numValue":74.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9061,"numValue":null,"references":[],"... | [{"id":7988,"numValue":4.0,"position":218,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,682 | train | mutant | 1,298 | 117 | 1,448 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K218F | K218F | 1 | 1 | 0 | 0 | 218 | K | F | 4 | CONSERVATION | 1STN | 140 | null | 218 | A | T | false | false | 140.289445 | 34.795556 | 2,557 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K136F | 47.5 | -5.5 | null | null | null | null | 72 | null | null | null | null | null | null | null | null | null | Unknown | 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|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["AUTOMUTE_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","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":9438,"numValue":47.5... | [{"id":7988,"numValue":4.0,"position":218,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,684 | train | mutant | 6,021 | 117 | 6,591 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K218A | K218A | 1 | 1 | 0 | 0 | 218 | K | A | 4 | CONSERVATION | 1STN | 140 | null | 218 | A | T | false | false | 140.289445 | 34.795556 | 12,896 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K136A | null | null | 4.7 | 0.9 | null | null | null | 0.7 | 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 | 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":46996,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46997,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46998,"numValue":0.98,"references":[],"strValue":nu... | [{"id":7988,"numValue":4.0,"position":218,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,685 | train | mutant | 6,021 | 117 | 6,591 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K218A | K218A | 1 | 1 | 0 | 0 | 218 | K | A | 4 | CONSERVATION | 1STN | 140 | null | 218 | A | T | false | false | 140.289445 | 34.795556 | 13,550 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K136A | null | null | 4.7 | 0.7 | null | null | null | 0.7 | 1.02 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":50080,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":50081,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50082,"numValue":1.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50083,"numValue":0.7,"r... | [{"id":7988,"numValue":4.0,"position":218,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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