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:7121 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,121 | train | mutant | 1,595 | 117 | 1,795 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152W | K152W | 1 | 1 | 0 | 0 | 152 | K | W | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 2,990 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate,Sodium sulfate, | 10 mM,10 mM, | null | 1STN_A:K70W | 50 | -3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate,Sodium sulfate,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"},{"numValue":n... | [{"datasets":[],"id":10855,"numValue":50.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10856,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7122 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,122 | train | mutant | 1,595 | 117 | 1,795 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152W | K152W | 1 | 1 | 0 | 0 | 152 | K | W | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 13,306 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K70W | null | null | 4.49 | 0.84 | null | null | null | 0.73 | 6.17 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":48886,"numValue":4.49,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48887,"numValue":0.84,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48888,"numValue":6.17,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48889,"numValue":0.73,"references":[],... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7123 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,123 | train | mutant | 1,595 | 117 | 1,795 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152W | K152W | 1 | 1 | 0 | 0 | 152 | K | W | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 13,309 | ProTherm | 7 | CD | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K70W | null | null | 4.87 | 0.15 | null | null | null | 0.75 | 6.49 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BU... | [{"datasets":[],"id":48901,"numValue":4.87,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48902,"numValue":0.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48903,"numValue":6.49,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48904,"numValue":0.75,"references":[],... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7124 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,124 | train | mutant | 2,164 | 117 | 2,458 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152C | K152C | 1 | 1 | 0 | 0 | 152 | K | C | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 4,257 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K70C | 50.2 | -2.8 | 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":15785,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15786,"numValue":-2.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15787,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7126 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,126 | train | mutant | 2,170 | 117 | 2,464 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152F | K152F | 1 | 1 | 0 | 0 | 152 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 4,265 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K70F | 53 | 0 | 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":15809,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15810,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15811,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,127 | train | mutant | 2,170 | 117 | 2,464 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152F | K152F | 1 | 1 | 0 | 0 | 152 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 13,349 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K70F | null | null | 5.3 | 0.2 | null | null | null | 0.83 | 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":49100,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49101,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49102,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49103,"numValue":0.83,... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,128 | train | mutant | 2,170 | 117 | 2,464 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152F | K152F | 1 | 1 | 0 | 0 | 152 | K | F | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 13,614 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K70F | null | null | 5.5 | 0 | null | null | null | 0.85 | 6.54 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":50368,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50369,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50370,"numValue":6.54,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":5037... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,129 | train | mutant | 6,002 | 117 | 6,572 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152A | K152A | 1 | 1 | 0 | 0 | 152 | K | A | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 12,876 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K70A | null | null | 5.5 | 0.1 | null | null | null | 0.77 | 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|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":46896,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46897,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46898,"numValue":1.04,"references... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,130 | train | mutant | 6,003 | 117 | 6,573 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152G | K152G | 1 | 1 | 0 | 0 | 152 | K | G | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 12,877 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K70G | null | null | 5.1 | 0.5 | null | null | null | 0.7 | 1.05 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46901,"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":46902,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46903,"numValue":1.05,"references... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,132 | train | mutant | 6,057 | 117 | 6,642 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K152Q | K152Q | 1 | 1 | 0 | 0 | 152 | K | Q | 5 | CONSERVATION | 1STN | 140 | null | 152 | A | S | true | false | 174.047636 | 18.135555 | 12,934 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K70Q | null | null | 5.1 | 0.3 | null | null | null | 0.79 | 6.47 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47186,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47187,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47188,"numValue":6.47,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4718... | [{"id":7922,"numValue":5.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,134 | train | mutant | 6,005 | 117 | 6,575 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K153G | K153G | 1 | 1 | 0 | 0 | 153 | K | G | 3 | CONSERVATION | 1STN | 140 | null | 153 | A | L | true | false | 134.806838 | 19.362222 | 12,879 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K71G | null | null | 4.5 | 1.1 | null | null | null | 0.58 | 1.12 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46911,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46912,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46913,"numValue":1.12,"references":[],"strValue":nu... | [{"id":7923,"numValue":3.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7135 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,135 | train | mutant | 6,250 | 117 | 6,845 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K153F | K153F | 1 | 1 | 0 | 0 | 153 | K | F | 3 | CONSERVATION | 1STN | 140 | null | 153 | A | L | true | false | 134.806838 | 19.362222 | 13,350 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K71F | null | null | 5.5 | 0 | null | null | null | 0.84 | 1 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49105,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49106,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":49107,"numValue":1... | [{"id":7923,"numValue":3.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7136 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,136 | train | mutant | 5,904 | 117 | 6,474 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L | I154L | 1 | 1 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 12,748 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L | null | null | 5.2 | 0.2 | null | null | null | 0.78 | 6.67 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46267,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46268,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46269,"numValue":6.67,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4627... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7137 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,137 | train | mutant | 5,905 | 117 | 6,475 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154M | I154M | 1 | 1 | 0 | 0 | 154 | I | M | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 12,749 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72M | null | null | 3.6 | 1.8 | null | null | null | 0.52 | 6.99 | 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":46272,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46273,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46274,"numValue":6.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46275,"numValue":0.52,... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,138 | train | mutant | 6,212 | 117 | 6,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154E | I154E | 1 | 1 | 0 | 0 | 154 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 13,214 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I72E | null | null | 4.8 | 4.7 | null | null | null | 1 | 4.9 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":3.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48452,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48453,"numValue":4.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48454,"numValue":4.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48455,"numValue":1.0,"references":[],"str... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7139 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,139 | train | mutant | 6,212 | 117 | 6,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154E | I154E | 1 | 1 | 0 | 0 | 154 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 13,215 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I72E | null | null | 6.3 | 5.4 | null | null | null | 1.2 | 5.1 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48457,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48458,"numValue":5.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48459,"numValue":5.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48460,"numValue":1.2,"references":[],"str... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,140 | train | mutant | 6,212 | 117 | 6,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154E | I154E | 1 | 1 | 0 | 0 | 154 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 13,216 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I72E | null | null | 5.2 | 6.5 | null | null | null | 1 | 5.5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48462,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48463,"numValue":6.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48464,"numValue":5.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48465,"numValue":1.0,"references":[],"str... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7141 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,141 | train | mutant | 6,212 | 117 | 6,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154E | I154E | 1 | 1 | 0 | 0 | 154 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 13,217 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I72E | null | null | 3.7 | 8.2 | null | null | null | 0.6 | 5.8 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48467,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48468,"numValue":8.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48469,"numValue":5.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48470,"numValue":0.6,"references":[],"str... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,142 | train | mutant | 6,212 | 117 | 6,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154E | I154E | 1 | 1 | 0 | 0 | 154 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 13,218 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I72E | null | null | 3.1 | 8.5 | null | null | null | 0.5 | 5.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48472,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48473,"numValue":8.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48474,"numValue":5.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48475,"numValue":0.5,"references":[],"str... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7143 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,143 | train | mutant | 6,309 | 117 | 6,909 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V | I154V | 1 | 1 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154 | A | E | true | false | 13.406159 | 10.5625 | 13,442 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V | null | null | 3.68 | 1.8 | null | null | null | 0.5 | 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 | 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":49557,"numValue":3.68,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49558,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49559,"numValue":1.02,"references":[],"strValue":n... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,145 | train | mutant | 7,209 | 117 | 7,864 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|Y167A | I154V|Y167A | 2 | 2 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|167 | A | E|T | true | true | 85.476667 | 14.347917 | 15,517 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:Y85A | null | null | null | 1.6 | null | null | null | null | 1.07 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":56965,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56966,"numValue":1.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56967,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7146 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,146 | train | mutant | 7,210 | 117 | 7,865 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|Y195A | I154V|Y195A | 2 | 2 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|195 | A | E|L | true | true | 91.197502 | 22.17875 | 15,518 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:Y113A | null | null | null | 0.94 | null | null | null | null | 1.1 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":56968,"numValue":0.94,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56969,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56970,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7965,"numValue":9.0,"position":195,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7147 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,147 | train | mutant | 7,264 | 117 | 7,919 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|I154V | E157V|I154V | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 154|157 | A | E | true | false | 10.102031 | 11.721805 | 15,574 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:E75V | null | null | null | 3.12 | null | null | null | null | 0.9 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57136,"numValue":3.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57137,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57138,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7148 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,148 | train | mutant | 7,270 | 117 | 7,925 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G161S|I154V | G161S|I154V | 2 | 2 | 0 | 0 | 161 | G | S | 8 | CONSERVATION | 1STN | 140 | null | 154|161 | A | E|S | true | false | 16.181476 | 11.7225 | 15,580 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:G79S | null | null | null | 3.61 | null | null | null | null | 0.98 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57154,"numValue":3.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57155,"numValue":0.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57156,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7149 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,149 | train | mutant | 8,021 | 117 | 8,748 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|I174V|V181I | I154V|I174V|V181I | 3 | 3 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|174|181 | A | E|H | true | false | 4.961413 | 8.843036 | 17,173 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:I92V 1STN_A:V99I | null | null | 4 | 1.4 | null | null | null | 0.56 | 7.18 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 984 | ARTICLE | Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. | 2,001 | 10.1021/bi011269d | 11705393 | Biochemistry;40;14012-9 | 2 | Chen 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":63269,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63270,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63271,"numValue":7.18,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63272,"numValue":0.56,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:7151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,151 | train | mutant | 8,023 | 117 | 8,750 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|I174V|V181L | I154V|I174V|V181L | 3 | 3 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|174|181 | A | E|H | true | false | 4.961413 | 8.843036 | 17,175 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:I92V 1STN_A:V99L | null | null | 3.4 | 2 | null | null | null | 0.47 | 7.25 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 984 | ARTICLE | Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. | 2,001 | 10.1021/bi011269d | 11705393 | Biochemistry;40;14012-9 | 2 | Chen 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":63279,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63280,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63281,"numValue":7.25,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63282,"numValue":0.47,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:7152 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,152 | train | mutant | 8,024 | 117 | 8,751 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L|I174V|V181L | I154L|I174V|V181L | 3 | 3 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154|174|181 | A | E|H | true | false | 4.961413 | 8.843036 | 17,176 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L 1STN_A:I92V 1STN_A:V99L | null | null | 4.3 | 1.1 | null | null | null | 0.63 | 6.86 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 984 | ARTICLE | Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. | 2,001 | 10.1021/bi011269d | 11705393 | Biochemistry;40;14012-9 | 2 | Chen 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":63284,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63285,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63286,"numValue":6.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63287,"numValue":0.63,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:7154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,154 | train | mutant | 8,026 | 117 | 8,753 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|I174L|V181L | I154V|I174L|V181L | 3 | 3 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|174|181 | A | E|H | true | false | 4.961413 | 8.843036 | 17,178 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:I92L 1STN_A:V99L | null | null | 3 | 2.4 | null | null | null | 0.41 | 7.38 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 984 | ARTICLE | Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. | 2,001 | 10.1021/bi011269d | 11705393 | Biochemistry;40;14012-9 | 2 | Chen 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":63294,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63295,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63296,"numValue":7.38,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63297,"numValue":0.41,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:7155 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,155 | train | mutant | 8,027 | 117 | 8,754 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L|I174L|V181I | I154L|I174L|V181I | 3 | 3 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154|174|181 | A | E|H | true | false | 4.961413 | 8.843036 | 17,179 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L 1STN_A:I92L 1STN_A:V99I | null | null | 4 | 1.4 | null | null | null | 0.65 | 6.2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 984 | ARTICLE | Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. | 2,001 | 10.1021/bi011269d | 11705393 | Biochemistry;40;14012-9 | 2 | Chen 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":63299,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63300,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63301,"numValue":6.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63302,"numValue":0.65,"references":[],"st... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:7156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,156 | train | mutant | 8,028 | 117 | 8,755 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|I174L|V181I | I154V|I174L|V181I | 3 | 3 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|174|181 | A | E|H | true | false | 4.961413 | 8.843036 | 17,180 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:I92L 1STN_A:V99I | null | null | 3.3 | 2.1 | null | null | null | 0.47 | 7.05 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 984 | ARTICLE | Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. | 2,001 | 10.1021/bi011269d | 11705393 | Biochemistry;40;14012-9 | 2 | Chen 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":63304,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63305,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63306,"numValue":7.05,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63307,"numValue":0.47,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:7157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,157 | train | mutant | 8,136 | 117 | 8,863 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L|I174L | I154L|I174L | 2 | 2 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154|174 | A | E | true | false | 7.173378 | 9.933125 | 17,288 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L 1STN_A:I92L | null | null | 4.7 | 0.7 | null | null | null | 0.74 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63844,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63845,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63846,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63847,"numValue":0.74,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7158 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,158 | train | mutant | 8,137 | 117 | 8,864 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L|I174V | I154L|I174V | 2 | 2 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154|174 | A | E | true | false | 7.173378 | 9.933125 | 17,289 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L 1STN_A:I92V | null | null | 4.7 | 0.7 | null | null | null | 0.69 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63849,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63850,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63851,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63852,"numValue":0.69,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,160 | train | mutant | 8,139 | 117 | 8,866 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|I174V | I154V|I174V | 2 | 2 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|174 | A | E | true | false | 7.173378 | 9.933125 | 17,291 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:I92V | null | null | 3.7 | 1.7 | null | null | null | 0.54 | 1.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63859,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63860,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63861,"numValue":1.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63862,"numValue":0.54,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,161 | train | mutant | 8,140 | 117 | 8,867 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L|V181I | I154L|V181I | 2 | 2 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154|181 | A | E|H | true | false | 6.971821 | 8.612679 | 17,292 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L 1STN_A:V99I | null | null | 4.9 | 0.5 | null | null | null | 0.76 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63864,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63865,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63866,"numValue":0.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63867,"numValue":0.76,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7162 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,162 | train | mutant | 8,141 | 117 | 8,868 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154L|V181L | I154L|V181L | 2 | 2 | 0 | 0 | 154 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 154|181 | A | E|H | true | false | 6.971821 | 8.612679 | 17,293 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72L 1STN_A:V99L | null | null | 4.6 | 0.8 | null | null | null | 0.71 | 0.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63869,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63870,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63871,"numValue":0.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63872,"numValue":0.71,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,163 | train | mutant | 8,142 | 117 | 8,869 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|V181I | I154V|V181I | 2 | 2 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|181 | A | E|H | true | false | 6.971821 | 8.612679 | 17,294 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:V99I | null | null | 4.2 | 1.2 | null | null | null | 0.61 | 1.05 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63874,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63875,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63876,"numValue":1.05,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63877,"numValue":0.61,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7164 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,164 | train | mutant | 8,143 | 117 | 8,870 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I154V|V181L | I154V|V181L | 2 | 2 | 0 | 0 | 154 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 154|181 | A | E|H | true | false | 6.971821 | 8.612679 | 17,295 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I72V 1STN_A:V99L | null | null | 3.7 | 1.7 | null | null | null | 0.53 | 1.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 986 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. | 2,001 | 10.1021/bi011268l | 11705392 | Biochemistry;40;14004-11 | 2 | Chen 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":63879,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63880,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63881,"numValue":1.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63882,"numValue":0.53,"references":[],"s... | [{"id":7924,"numValue":8.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7165 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,165 | train | mutant | 375 | 117 | 414 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155G | E155G | 1 | 1 | 0 | 0 | 155 | E | G | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 639 | ProTherm | 7 | DSC | Thermal | phosphate | null | 1STN_A:E73G | 36.8 | -15.2 | null | null | 65.6 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 70 | ARTICLE | Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis. | 2,001 | 10.1074/jbc.M106620200 | 11598114 | J Biol Chem;276;46039-45 | 8 | Leung K W|Liaw Y C|Chan S C|Lo H Y|Musayev F N|Chen J Z|Fang H J|Chen H M | [{"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":"1STN_A:E73G","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2523,"numValue":36.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2524,"numValue":-15.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2525,"numValue":65.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,166 | train | mutant | 375 | 117 | 414 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155G | E155G | 1 | 1 | 0 | 0 | 155 | E | G | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 12,839 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E73G | null | null | 2.9 | 2.7 | null | null | null | 0.39 | 1.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46711,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46712,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46713,"numValue":1.03,"references":[],"strValue":nu... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7168 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,168 | train | mutant | 1,285 | 117 | 1,435 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155F | E155F | 1 | 1 | 0 | 0 | 155 | E | F | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 2,544 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E73F | 48.8 | -4.2 | null | null | null | null | 79 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9386,"numValue":48.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9387,"numValue":-4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,169 | train | mutant | 1,285 | 117 | 1,435 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155F | E155F | 1 | 1 | 0 | 0 | 155 | E | F | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 13,351 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E73F | null | null | 4.4 | 1.1 | null | null | null | 0.73 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49110,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49111,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49112,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49113,"numValue":0.73,... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7170 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,170 | train | mutant | 5,968 | 117 | 6,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155A | E155A | 1 | 1 | 0 | 0 | 155 | E | A | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 12,838 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E73A | null | null | 4.2 | 1.2 | null | null | null | 0.59 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46706,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46707,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46708,"numValue":1.01,"references":[],"strValue":nu... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,171 | train | mutant | 5,968 | 117 | 6,538 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155A | E155A | 1 | 1 | 0 | 0 | 155 | E | A | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 13,135 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E73A | null | null | -1.6 | null | null | null | null | null | 1 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48089,"numValue":-1.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48090,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48091,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7172 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,172 | train | mutant | 6,058 | 117 | 6,643 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155K | E155K | 1 | 1 | 0 | 0 | 155 | E | K | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 12,935 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E73K | null | null | 3.3 | 2.1 | null | null | null | 0.51 | 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":47191,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47192,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47193,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47194,"numValue":0.51,"... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7173 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,173 | train | mutant | 6,059 | 117 | 6,644 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155Q | E155Q | 1 | 1 | 0 | 0 | 155 | E | Q | 4 | CONSERVATION | 1STN | 140 | null | 155 | A | E | true | false | 49.443637 | 14.427778 | 12,936 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E73Q | null | null | 4.7 | 0.7 | null | null | null | 0.73 | 6.47 | 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":47196,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47197,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47198,"numValue":6.47,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47199,"numValue":0.73,... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7174 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,174 | train | mutant | 7,202 | 117 | 7,857 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155A|V156A | E155A|V156A | 2 | 2 | 0 | 0 | 155 | E | A | 4 | CONSERVATION | 1STN | 140 | null | 155|156 | A | E | true | false | 24.721818 | 13.288889 | 15,507 | ProTherm | 7 | CD | GdnHCl | NaH2PO4 | 10 mM | 20 | NaCl | 100 mM | 1STN_A:E73A 1STN_A:V74A | null | null | null | 5.2 | null | null | null | null | 0.98 | null | null | null | null | null | null | null | Unknown | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 935 | ARTICLE | Structural and energetic differences between insertions and substitutions in staphylococcal nuclease. | 1,992 | 10.1002/prot.340130206 | 1620695 | Proteins;13;132-40 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":56933,"numValue":5.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56934,"numValue":0.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56935,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7175 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,175 | train | mutant | 7,325 | 117 | 7,995 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155G|D159G | E155G|D159G | 2 | 2 | 0 | 0 | 155 | E | G | 4 | CONSERVATION | 1STN | 140 | null | 155|159 | A | E|L | true | false | 26.443588 | 14.370139 | 15,686 | ProTherm | 7 | DSC | Thermal | phosphate | null | 1STN_A:E73G 1STN_A:D77G | 30 | -22 | null | null | 45 | -0.7 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 70 | ARTICLE | Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis. | 2,001 | 10.1074/jbc.M106620200 | 11598114 | J Biol Chem;276;46039-45 | 8 | Leung K W|Liaw Y C|Chan S C|Lo H Y|Musayev F N|Chen J Z|Fang H J|Chen H M | [{"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":"1STN_A:E73G 1STN_A:D77G","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":57567,"numValue":30.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57568,"numValue":-22.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57569,"numValue":45.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57570,"numValue":-0.7,"references":[... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7176 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,176 | train | mutant | 7,326 | 117 | 7,996 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155G|E157G | E155G|E157G | 2 | 2 | 0 | 0 | 155 | E | G | 4 | CONSERVATION | 1STN | 140 | null | 155|157 | A | E | true | false | 28.12077 | 13.654444 | 15,687 | ProTherm | 7 | DSC | Thermal | phosphate | null | 1STN_A:E73G 1STN_A:E75G | 27.5 | -24.5 | null | null | 34.3 | -0.8 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 70 | ARTICLE | Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis. | 2,001 | 10.1074/jbc.M106620200 | 11598114 | J Biol Chem;276;46039-45 | 8 | Leung K W|Liaw Y C|Chan S C|Lo H Y|Musayev F N|Chen J Z|Fang H J|Chen H M | [{"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":"1STN_A:E73G 1STN_A:E75G","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":57572,"numValue":27.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57573,"numValue":-24.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57574,"numValue":34.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57575,"numValue":-0.8,"references":[... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7177 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,177 | train | mutant | 7,328 | 117 | 7,998 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E155G|E157G|D159G | E155G|E157G|D159G | 3 | 3 | 0 | 0 | 155 | E | G | 4 | CONSERVATION | 1STN | 140 | null | 155|157|159 | A | E|L | true | false | 19.895026 | 13.873796 | 15,689 | ProTherm | 7 | DSC | Thermal | phosphate | null | 1STN_A:E73G 1STN_A:E75G 1STN_A:D77G | 25.1 | -26.9 | null | null | 29.4 | -1.3 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 70 | ARTICLE | Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis. | 2,001 | 10.1074/jbc.M106620200 | 11598114 | J Biol Chem;276;46039-45 | 8 | Leung K W|Liaw Y C|Chan S C|Lo H Y|Musayev F N|Chen J Z|Fang H J|Chen H M | [{"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":"1STN_A:E73G 1STN_A:E75G 1STN_A:D77G","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":57582,"numValue":25.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57583,"numValue":-26.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57584,"numValue":29.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57585,"numValue":-1.3,"references":[... | [{"id":7925,"numValue":4.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:7178 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,178 | train | mutant | 1,221 | 117 | 1,371 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156T | V156T | 1 | 1 | 0 | 0 | 156 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 2,384 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V74T | 34.4 | -18.3 | null | null | null | null | 64 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|EASE-MM_S1676.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","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv"],"id":8746,"numValue":34.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv"],"id":8747,"numValue":-18.3,"references":[],"strValue":null,"type":"DTM"},{"datas... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7179 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,179 | train | mutant | 1,221 | 117 | 1,371 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156T | V156T | 1 | 1 | 0 | 0 | 156 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 2,479 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V74T | 36.1 | -16.9 | null | null | null | null | 62 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | STRUM_Q3421.csv|AUTOMUTE_S1925.csv|Broom_S605.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|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":["STRUM_Q3421.csv"],"id":9126,"numValue":36.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","Broom_S605.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","SVM-WI... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7180 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,180 | train | mutant | 1,221 | 117 | 1,371 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156T | V156T | 1 | 1 | 0 | 0 | 156 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,482 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V74T | null | null | 1.8 | 3.8 | null | null | null | 0.24 | 1.14 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49756,"numValue":1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49757,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49758,"numValue":1.14,"references":[],"strValue":nu... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7181 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,181 | train | mutant | 5,891 | 117 | 6,461 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156I | V156I | 1 | 1 | 0 | 0 | 156 | V | I | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 12,734 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V74I | null | null | 3.6 | 1.8 | null | null | null | 0.51 | 7.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46197,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46198,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46199,"numValue":7.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46200,"numValue":0.51,... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7182 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,182 | train | mutant | 5,892 | 117 | 6,462 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156L | V156L | 1 | 1 | 0 | 0 | 156 | V | L | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 12,735 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V74L | null | null | 4.2 | 1.2 | null | null | null | 0.66 | 6.35 | 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":46202,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46203,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46204,"numValue":6.35,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46205,"numValue":0.66,... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7183 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,183 | train | mutant | 6,213 | 117 | 6,807 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156E | V156E | 1 | 1 | 0 | 0 | 156 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,219 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V74E | null | null | 4.1 | 5.4 | null | null | null | 0.9 | 4.7 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48477,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48478,"numValue":5.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48479,"numValue":4.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48480,"numValue":0.9,"references":[],"str... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7184 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,184 | train | mutant | 6,213 | 117 | 6,807 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156E | V156E | 1 | 1 | 0 | 0 | 156 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,220 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V74E | null | null | 5.7 | 6.1 | null | null | null | 1 | 5.5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48482,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48483,"numValue":6.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48484,"numValue":5.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48485,"numValue":1.0,"references":[],"str... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7185 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,185 | train | mutant | 6,213 | 117 | 6,807 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156E | V156E | 1 | 1 | 0 | 0 | 156 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,221 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V74E | null | null | 4.9 | 6.8 | null | null | null | 0.8 | 5.8 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48487,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":48488,"numValue":6.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48489,"numValue":5.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48490,"numValue":0.8,"re... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7186 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,186 | train | mutant | 6,213 | 117 | 6,807 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156E | V156E | 1 | 1 | 0 | 0 | 156 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,222 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V74E | null | null | 2.7 | 9.2 | null | null | null | 0.5 | 5.5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":7.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48492,"numValue":2.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48493,"numValue":9.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48494,"numValue":5.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48495,"numValue":0.5,"references":[],"str... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7188 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,188 | train | mutant | 6,213 | 117 | 6,807 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156E | V156E | 1 | 1 | 0 | 0 | 156 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,224 | ProTherm | 9.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V74E | null | null | 1.2 | 9.1 | null | null | null | 0.2 | 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":9.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48502,"numValue":1.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48503,"numValue":9.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48504,"numValue":5.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48505,"numValue":0.2,"references":[],"str... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7189 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,189 | train | mutant | 6,296 | 117 | 6,896 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V156A | V156A | 1 | 1 | 0 | 0 | 156 | V | A | 7 | CONSERVATION | 1STN | 140 | null | 156 | A | E | true | false | 0 | 12.15 | 13,428 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V74A | null | null | 2.38 | 3.1 | null | null | null | 0.3 | 1.13 | 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":49488,"numValue":2.38,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49489,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49490,"numValue":1.13,"references":[],"strValue":n... | [{"id":7926,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7191 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,191 | train | mutant | 1,605 | 117 | 1,805 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157A | E157A | 1 | 1 | 0 | 0 | 157 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 3,008 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:E75A | 48.5 | -5.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 268 | ARTICLE | Energetics of denaturation and m values of staphylococcal nuclease mutants. | 1,995 | 10.1021/bi00006a025 | 7849061 | Biochemistry;34;2034-41 | 2 | Privalov P L|Carra J H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10915,"numValue":48.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10916,"numValue":-5.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Saraboji_S22... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7192 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,192 | train | mutant | 1,605 | 117 | 1,805 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157A | E157A | 1 | 1 | 0 | 0 | 157 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 11,072 | ProTherm | 5.6 | Fluorescence | GdnHCl | Sodium acetate | 50 mM | 25 | NaCl | 100 mM | 1STN_A:E75A | null | null | 2.1 | null | null | null | null | null | 5 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":5.6,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":38119,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38120,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38121,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7193 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,193 | train | mutant | 1,605 | 117 | 1,805 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157A | E157A | 1 | 1 | 0 | 0 | 157 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 11,073 | ProTherm | 5.2 | Fluorescence | GdnHCl | Sodium acetate | 50 mM | 25 | NaCl | 100 mM | 1STN_A:E75A | null | null | 2 | null | null | null | null | null | 4.3 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":5.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":38122,"numValue":2.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38123,"numValue":4.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38124,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7194 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,194 | train | mutant | 1,605 | 117 | 1,805 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157A | E157A | 1 | 1 | 0 | 0 | 157 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 12,840 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75A | null | null | 3.4 | 2.2 | null | null | null | 0.62 | 0.78 | 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":46716,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46717,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46718,"numValue":0.78,"references":[],"strValue":nu... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7195 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,195 | train | mutant | 1,605 | 117 | 1,805 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157A | E157A | 1 | 1 | 0 | 0 | 157 | E | A | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 13,541 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75A | null | null | 3.3 | null | null | null | null | null | 5.3 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"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":50045,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":50046,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50047,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7196 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,196 | train | mutant | 1,606 | 117 | 1,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157G | E157G | 1 | 1 | 0 | 0 | 157 | E | G | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 3,009 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:E75G | 38.9 | -15.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 268 | ARTICLE | Energetics of denaturation and m values of staphylococcal nuclease mutants. | 1,995 | 10.1021/bi00006a025 | 7849061 | Biochemistry;34;2034-41 | 2 | Privalov P L|Carra J H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10918,"numValue":38.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10919,"numValue":-15.2,"references":[],"strValue":nu... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7197 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,197 | train | mutant | 1,606 | 117 | 1,806 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157G | E157G | 1 | 1 | 0 | 0 | 157 | E | G | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 12,841 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75G | null | null | 2.1 | 3.5 | null | null | null | 0.31 | 0.93 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | 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":46721,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46722,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46723,"numValue":0.93,"references":[],"strValue":nu... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7198 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,198 | train | mutant | 1,619 | 117 | 1,820 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V | E157V | 1 | 1 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 3,041 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:E75V | 47.5 | -6.6 | null | null | 69.9 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11056,"numValue":47.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11057,"numValue":-6.6,"references":[],"strValue":nul... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:7199 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,199 | train | mutant | 1,619 | 117 | 1,820 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V | E157V | 1 | 1 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 3,042 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:E75V | 60.8 | null | null | null | 69.9 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11061,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv"],"id":11062,"numValue":69.9,"references":[],"strValue":null,"type":"DH"},{"datasets"... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:7201 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,201 | train | mutant | 6,060 | 117 | 6,645 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157K | E157K | 1 | 1 | 0 | 0 | 157 | E | K | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 12,937 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E75K | null | null | 3.1 | 2.3 | null | null | null | 0.49 | 6.27 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47201,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47202,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47203,"numValue":6.27,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47204,"numValue":0.49,... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7202 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,202 | train | mutant | 6,061 | 117 | 6,646 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157Q | E157Q | 1 | 1 | 0 | 0 | 157 | E | Q | 8 | CONSERVATION | 1STN | 140 | null | 157 | A | E | true | false | 6.797904 | 12.881111 | 12,938 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:E75Q | null | null | 4.7 | 0.7 | null | null | null | 0.74 | 6.27 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 828 | ARTICLE | Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. | 2,003 | 10.1021/bi0266434 | 12549934 | Biochemistry;42;1118-28 | 5 | Stites Wesley E|Schwehm Jeffery M|Fitch Carolyn A|Dang Bao N|Garc?a-Moreno E Bertrand | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47206,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47207,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47208,"numValue":6.27,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47209,"numValue":0.74,... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7203 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,203 | train | mutant | 7,229 | 117 | 7,884 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|G161S | E157V|G161S | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|161 | A | E|S | true | false | 12.877349 | 12.881806 | 15,539 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:G79S | null | null | null | 4.67 | null | null | null | null | 0.56 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57031,"numValue":4.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57032,"numValue":0.56,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57033,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7931,"numValue":6.0,"position":161,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7204 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,204 | train | mutant | 7,230 | 117 | 7,885 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|P199L | E157V|P199L | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|199 | A | E|T | true | false | 34.841753 | 17.592698 | 15,540 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:P117L | null | null | null | 1.61 | null | null | null | null | 0.78 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57034,"numValue":1.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57035,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57036,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7969,"numValue":7.0,"position":199,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7205 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,205 | train | mutant | 7,243 | 117 | 7,898 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|A172S | E157V|A172S | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|172 | A | E | true | false | 3.398952 | 10.348555 | 15,553 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:A90S | null | null | null | 3.6 | null | null | null | null | 0.97 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57073,"numValue":3.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57074,"numValue":0.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57075,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7206 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,206 | train | mutant | 7,265 | 117 | 7,920 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|Y167A | E157V|Y167A | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|167 | A | E|T | true | true | 82.172539 | 15.507222 | 15,575 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:Y85A | null | null | null | 2.51 | null | null | null | null | 0.82 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57139,"numValue":2.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57140,"numValue":0.82,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57141,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7937,"numValue":9.0,"position":167,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7207 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,207 | train | mutant | 7,266 | 117 | 7,921 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|I174V | E157V|I174V | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|174 | A | E | true | false | 3.86925 | 11.09243 | 15,576 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:I92V | null | null | null | 2.05 | null | null | null | null | 0.91 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57142,"numValue":2.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57143,"numValue":0.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57144,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7208 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,208 | train | mutant | 7,267 | 117 | 7,922 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|Y195A | E157V|Y195A | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|195 | A | E|L | true | true | 87.893375 | 23.338056 | 15,577 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:Y113A | null | null | null | 1.55 | null | null | null | null | 0.92 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57145,"numValue":1.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57146,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57147,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7965,"numValue":9.0,"position":195,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7209 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,209 | train | mutant | 7,268 | 117 | 7,923 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157V|A212G | E157V|A212G | 2 | 2 | 0 | 0 | 157 | E | V | 8 | CONSERVATION | 1STN | 140 | null | 157|212 | A | E|H | true | false | 31.899406 | 13.364556 | 15,578 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E75V 1STN_A:A130G | null | null | null | 3.4 | null | null | null | null | 0.74 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 842 | ARTICLE | Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. | 1,993 | 10.1021/bi00089a032 | 8399139 | Biochemistry;32;10131-9 | 2 | Shortle D|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":57148,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57149,"numValue":0.74,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57150,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7982,"numValue":4.0,"position":212,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7210 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,210 | train | mutant | 7,327 | 117 | 7,997 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E157G|D159G | E157G|D159G | 2 | 2 | 0 | 0 | 157 | E | G | 8 | CONSERVATION | 1STN | 140 | null | 157|159 | A | E|L | true | false | 5.120721 | 13.596805 | 15,688 | ProTherm | 7 | DSC | Thermal | phosphate | null | 1STN_A:E75G 1STN_A:D77G | 32 | -20 | null | null | 35.6 | -1.2 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 70 | ARTICLE | Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis. | 2,001 | 10.1074/jbc.M106620200 | 11598114 | J Biol Chem;276;46039-45 | 8 | Leung K W|Liaw Y C|Chan S C|Lo H Y|Musayev F N|Chen J Z|Fang H J|Chen H M | [{"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":"1STN_A:E75G 1STN_A:D77G","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":57577,"numValue":32.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57578,"numValue":-20.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57579,"numValue":35.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":57580,"numValue":-1.2,"references":[... | [{"id":7927,"numValue":8.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7211 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,211 | train | mutant | 6,196 | 117 | 6,790 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F158A | F158A | 1 | 1 | 0 | 0 | 158 | F | A | 6 | CONSERVATION | 1STN | 140 | null | 158 | A | E | true | false | 19.691863 | 13.565455 | 13,136 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:F76A | null | null | -4.1 | null | null | null | null | null | 1.07 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48092,"numValue":-4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48093,"numValue":1.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48094,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7928,"numValue":6.0,"position":158,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7214 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,214 | train | mutant | 6,197 | 117 | 6,791 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F158G | F158G | 1 | 1 | 0 | 0 | 158 | F | G | 6 | CONSERVATION | 1STN | 140 | null | 158 | A | E | true | false | 19.691863 | 13.565455 | 13,471 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:F76G | null | null | 0.78 | 4.7 | null | null | null | 0.1 | 1.05 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 850 | ARTICLE | Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. | 1,990 | 10.1021/bi00487a007 | 2261461 | Biochemistry;29;8033-41 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49702,"numValue":0.78,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49703,"numValue":4.7,"references":[],"strValue":null,"... | [{"id":7928,"numValue":6.0,"position":158,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7215 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,215 | train | mutant | 6,884 | 117 | 7,526 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F158V|H206L | F158V|H206L | 2 | 2 | 0 | 0 | 158 | F | V | 6 | CONSERVATION | 1STN | 140 | null | 158|206 | A | E|H | true | false | 57.368669 | 19.570227 | 14,714 | ProTherm | 5.21 | NMR | Thermal | Unknown | null | NaCl | 0.3 M | 1STN_A:F76V 1STN_A:H124L | 47 | -0.8 | null | null | null | null | 52.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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":5.21,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.3 M","type":"ION_CONC"},{"numVa... | [{"datasets":[],"id":54407,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54408,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54409,"numValue":52.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54410,"numValue":null,"references":... | [{"id":7928,"numValue":6.0,"position":158,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7216 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,216 | train | mutant | 6,884 | 117 | 7,526 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F158V|H206L | F158V|H206L | 2 | 2 | 0 | 0 | 158 | F | V | 6 | CONSERVATION | 1STN | 140 | null | 158|206 | A | E|H | true | false | 57.368669 | 19.570227 | 15,112 | ProTherm | 5.21 | NMR | Thermal | Unknown | 40 | NaCl | 0.3 M | 1STN_A:F76V 1STN_A:H124L | null | null | 1.4 | 0 | null | 0 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|DDG|REVERSIBILITY | 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":5.21,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":55448,"numValue":0.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55449,"numValue":1.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55450,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55451,"numValue":null,"references":[],"... | [{"id":7928,"numValue":6.0,"position":158,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7976,"numValue":4.0,"position":206,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7217 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,217 | train | mutant | 7,374 | 117 | 8,044 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F158W|W222H | F158W|W222H | 2 | 2 | 0 | 0 | 158 | F | W | 6 | CONSERVATION | 1STN | 140 | null | 158|222 | A | E|G | true | false | 38.683067 | 17.913442 | 15,763 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | null | NaCl | 50 mM | 1STN_A:F76W 1STN_A:W140H | 56.6 | null | null | null | null | null | 77.6 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":57875,"numValue":56.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57876,"numValue":77.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":57877,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7928,"numValue":6.0,"position":158,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7218 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,218 | train | mutant | 7,374 | 117 | 8,044 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | F158W|W222H | F158W|W222H | 2 | 2 | 0 | 0 | 158 | F | W | 6 | CONSERVATION | 1STN | 140 | null | 158|222 | A | E|G | true | false | 38.683067 | 17.913442 | 17,299 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | 20 | NaCl | 50 mM | 1STN_A:F76W 1STN_A:W140H | null | null | 5.1 | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BU... | [{"datasets":[],"id":63894,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63895,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63896,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7928,"numValue":6.0,"position":158,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7219 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,219 | train | mutant | 376 | 117 | 415 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159G | D159G | 1 | 1 | 0 | 0 | 159 | D | G | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 640 | ProTherm | 7 | DSC | Thermal | phosphate | null | 1STN_A:D77G | 43.9 | -8.1 | null | null | 62.1 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 70 | ARTICLE | Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis. | 2,001 | 10.1074/jbc.M106620200 | 11598114 | J Biol Chem;276;46039-45 | 8 | Leung K W|Liaw Y C|Chan S C|Lo H Y|Musayev F N|Chen J Z|Fang H J|Chen H M | [{"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":"1STN_A:D77G","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2527,"numValue":43.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2528,"numValue":-8.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2529,"numValue":62.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7220 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,220 | train | mutant | 376 | 117 | 415 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159G | D159G | 1 | 1 | 0 | 0 | 159 | D | G | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 12,819 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77G | null | null | 4.4 | 2.2 | null | null | null | 0.6 | 0.79 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46611,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46612,"numValue":2.2,"references":[],"strValue":null,"t... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7221 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,221 | train | mutant | 376 | 117 | 415 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159G | D159G | 1 | 1 | 0 | 0 | 159 | D | G | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 13,139 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77G | null | null | -2.2 | null | null | null | null | null | 0.83 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48101,"numValue":-2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48102,"numValue":0.83,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48103,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7222 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,222 | train | mutant | 376 | 117 | 415 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159G | D159G | 1 | 1 | 0 | 0 | 159 | D | G | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 13,575 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77G | null | null | 3.2 | 2.2 | null | null | null | 0.6 | 0.79 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":50205,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":50206,"numValue":2.2,"references":[],"strValue":null,"t... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7223 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,223 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 3,039 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:D77A | 43.4 | -10.7 | null | null | 65.6 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DTM|DH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q306.csv|STRUM_Q3421.c... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","Saraboji_S2204.csv"],"id":11047,"numValue":43.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":11048,"numValue":-10.7,"references":[],"strValu... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:7224 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,224 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 3,040 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 1STN_A:D77A | 72.6 | null | null | null | 65.6 | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DH|STATE|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11052,"numValue":72.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11053,"numValue":65.6,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S196... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:7225 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,225 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 11,074 | ProTherm | 5.6 | Fluorescence | GdnHCl | Sodium acetate | 50 mM | 25 | NaCl | 100 mM | 1STN_A:D77A | null | null | 2 | null | null | null | null | null | 5.1 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":5.6,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":38125,"numValue":2.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38126,"numValue":5.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38127,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7226 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,226 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 11,075 | ProTherm | 5.2 | Fluorescence | GdnHCl | Sodium acetate | 50 mM | 25 | NaCl | 100 mM | 1STN_A:D77A | null | null | 2.3 | null | null | null | null | null | 4.5 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":5.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":38128,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38129,"numValue":4.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38130,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7227 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,227 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 12,818 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77A | null | null | 2.5 | 3.1 | null | null | null | 0.45 | 0.76 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 827 | ARTICLE | Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. | 1,996 | 10.1021/bi960171+ | 8639591 | Biochemistry;35;6443-9 | 3 | Shortle D|Garcia-Moreno B|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46606,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46607,"numValue":3.1,"references":[],"strValue":null,"t... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,228 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 13,138 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77A | null | null | -3.2 | null | null | null | null | null | 0.78 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":48098,"numValue":-3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48099,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48100,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,229 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 13,542 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77A | null | null | 2.4 | null | null | null | null | null | 5.2 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"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":50048,"numValue":2.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":50049,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50050,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7230 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,230 | train | mutant | 1,618 | 117 | 1,819 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159A | D159A | 1 | 1 | 0 | 0 | 159 | D | A | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 13,574 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D77A | null | null | 2.3 | 3.1 | null | null | null | 0.45 | 0.75 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":50200,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":50201,"numValue":3.1,"references":[],"strValue":null,"t... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,231 | train | mutant | 6,062 | 117 | 6,647 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159K | D159K | 1 | 1 | 0 | 0 | 159 | D | K | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 12,939 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:D77K | null | null | 1.9 | 3.5 | null | null | null | 0.35 | 5.54 | 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":47211,"numValue":1.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47212,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47213,"numValue":5.54,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47214,"numValue":0.35,... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7232 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,232 | train | mutant | 6,063 | 117 | 6,648 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D159N | D159N | 1 | 1 | 0 | 0 | 159 | D | N | 9 | CONSERVATION | 1STN | 140 | null | 159 | A | L | false | false | 3.443539 | 14.3125 | 12,940 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:D77N | null | null | 2.5 | 2.9 | null | null | null | 0.44 | 5.74 | 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":47216,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47217,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47218,"numValue":5.74,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47219,"numValue":0.44,... | [{"id":7929,"numValue":9.0,"position":159,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7233 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,233 | train | mutant | 2,165 | 117 | 2,459 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K160C | K160C | 1 | 1 | 0 | 0 | 160 | K | C | 5 | CONSERVATION | 1STN | 140 | null | 160 | A | S | false | false | 129.372856 | 29.735555 | 4,258 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:K78C | 53.4 | 0.4 | 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":15788,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15789,"numValue":0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15790,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7930,"numValue":5.0,"position":160,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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