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:7345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,345 | train | mutant | 111 | 117 | 122 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172S | A172S | 1 | 1 | 0 | 0 | 172 | A | S | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,143 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A90S | null | null | -2 | null | null | null | null | null | 1.1 | 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":48113,"numValue":-2.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48114,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48115,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,346 | train | mutant | 111 | 117 | 122 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172S | A172S | 1 | 1 | 0 | 0 | 172 | A | S | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,304 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A90S | null | null | null | 1.9 | 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":48878,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48879,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48880,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,349 | train | mutant | 6,097 | 117 | 6,685 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172G | A172G | 1 | 1 | 0 | 0 | 172 | A | G | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,008 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A90G | null | null | 3.5 | 2 | null | null | null | 0.53 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47511,"numValue":3.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47512,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47513,"numValue":0.96,"references":[],"strValue":nu... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,350 | train | mutant | 6,098 | 117 | 6,686 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172V | A172V | 1 | 1 | 0 | 0 | 172 | A | V | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,009 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A90V | null | null | 5.3 | 0.2 | null | null | null | 0.84 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47516,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47517,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47518,"numValue":0.92,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4751... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,351 | train | mutant | 6,214 | 117 | 6,808 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172E | A172E | 1 | 1 | 0 | 0 | 172 | A | E | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,225 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A90E | null | null | 1.9 | 7.5 | null | null | null | 0.4 | 4.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48507,"numValue":1.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48508,"numValue":7.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48509,"numValue":4.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48510,"numValue":0.4,"references":[],"str... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7353 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,353 | train | mutant | 6,214 | 117 | 6,808 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172E | A172E | 1 | 1 | 0 | 0 | 172 | A | E | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,227 | ProTherm | 5.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A90E | null | null | 4 | 7.7 | null | null | null | 0.7 | 5.7 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":5.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48517,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":48518,"numValue":7.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48519,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48520,"numValue":0.7,"r... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,354 | train | mutant | 6,214 | 117 | 6,808 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172E | A172E | 1 | 1 | 0 | 0 | 172 | A | E | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,228 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A90E | null | null | 3.3 | 8.6 | null | null | null | 0.6 | 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":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":48522,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48523,"numValue":8.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48524,"numValue":5.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48525,"numValue":0.6,"references":[],"str... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,355 | train | mutant | 6,214 | 117 | 6,808 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A172E | A172E | 1 | 1 | 0 | 0 | 172 | A | E | 8 | CONSERVATION | 1STN | 140 | null | 172 | A | E | true | false | 0 | 7.816 | 13,229 | ProTherm | 9.1 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:A90E | null | null | 3.3 | 8.2 | null | null | null | 0.6 | 5.7 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":9.1,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48527,"numValue":3.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48528,"numValue":8.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48529,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48530,"numValue":0.6,"references":[],"str... | [{"id":7942,"numValue":8.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7356 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,356 | train | mutant | 1,233 | 117 | 1,383 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173F | Y173F | 1 | 1 | 0 | 0 | 173 | Y | F | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 2,396 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y91F | 45.5 | -7.2 | null | null | null | null | 60 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|Broom_S605.csv|HotMuSiC_S1626.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"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":["PoPMuSiC-2.0_S2648.csv"],"id":8794,"numValue":45.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv"],"id":8795,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv"],... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,357 | train | mutant | 1,233 | 117 | 1,383 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173F | Y173F | 1 | 1 | 0 | 0 | 173 | Y | F | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 2,491 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y91F | 46.6 | -6.4 | null | null | null | null | 59 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9174,"numValue":46.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9175,"numValue":-6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9176,"numValue":59.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9177,"numValue":null,"references":[],"... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7358 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,358 | train | mutant | 1,233 | 117 | 1,383 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173F | Y173F | 1 | 1 | 0 | 0 | 173 | Y | F | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,499 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y91F | null | null | 3.2 | 2.4 | null | null | null | 0.51 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49841,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49842,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49843,"numValue":0.94,"references":[],"strValue":nu... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,359 | train | mutant | 1,239 | 117 | 1,389 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173L | Y173L | 1 | 1 | 0 | 0 | 173 | Y | L | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 2,402 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y91L | 38.6 | -14.1 | null | null | null | null | 50 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8818,"numValue":38.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8819,"numValue":-14.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8820,"numValue":50.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8821,"numValue":null,"references":[],... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7361 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,361 | train | mutant | 1,239 | 117 | 1,389 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173L | Y173L | 1 | 1 | 0 | 0 | 173 | Y | L | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,506 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y91L | null | null | 1.7 | 3.9 | null | null | null | 0.27 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49873,"numValue":1.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49874,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49875,"numValue":0.96,"references":[],"strValue":nu... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,362 | train | mutant | 6,198 | 117 | 6,792 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173S | Y173S | 1 | 1 | 0 | 0 | 173 | Y | S | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,144 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y91S | null | null | -5.3 | null | null | null | null | null | 1.08 | 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":48116,"numValue":-5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48117,"numValue":1.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48118,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,363 | train | mutant | 6,215 | 117 | 6,809 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173E | Y173E | 1 | 1 | 0 | 0 | 173 | Y | E | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,230 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:Y91E | null | null | 4.5 | 5 | null | null | null | 1 | 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":48532,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48533,"numValue":5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48534,"numValue":4.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48535,"numValue":1.0,"references":[],"str... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,364 | train | mutant | 6,215 | 117 | 6,809 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173E | Y173E | 1 | 1 | 0 | 0 | 173 | Y | E | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,231 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:Y91E | null | null | 6.3 | 5.4 | null | null | null | 1.2 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":4.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48537,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48538,"numValue":5.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48539,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48540,"numValue":1.2,"references":[],"str... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,365 | train | mutant | 6,215 | 117 | 6,809 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173E | Y173E | 1 | 1 | 0 | 0 | 173 | Y | E | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,232 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:Y91E | null | null | 4.4 | 7.3 | null | null | null | 0.9 | 5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48542,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48543,"numValue":7.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48544,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48545,"numValue":0.9,"references":[],"str... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,366 | train | mutant | 6,215 | 117 | 6,809 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173E | Y173E | 1 | 1 | 0 | 0 | 173 | Y | E | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,233 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:Y91E | null | null | 3.2 | 8.7 | null | null | null | 0.6 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48547,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48548,"numValue":8.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48549,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48550,"numValue":0.6,"references":[],"str... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,367 | train | mutant | 6,215 | 117 | 6,809 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173E | Y173E | 1 | 1 | 0 | 0 | 173 | Y | E | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,234 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:Y91E | null | null | 3 | 8.6 | null | null | null | 0.6 | 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":9.0,"strValue":null,"type":"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":48552,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48553,"numValue":8.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48554,"numValue":5.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48555,"numValue":0.6,"references":[],"str... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,368 | train | mutant | 6,326 | 117 | 6,926 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y173A | Y173A | 1 | 1 | 0 | 0 | 173 | Y | A | 9 | CONSERVATION | 1STN | 140 | null | 173 | A | E | true | false | 0 | 8.310833 | 13,462 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y91A | null | null | 0.18 | 5.3 | null | null | null | 0 | 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 | 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":49657,"numValue":0.18,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49658,"numValue":5.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49659,"numValue":1.01,"references":[],"strValue":n... | [{"id":7943,"numValue":9.0,"position":173,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,369 | train | mutant | 5,906 | 117 | 6,476 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174L | I174L | 1 | 1 | 0 | 0 | 174 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 12,750 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92L | null | null | 4.8 | 0.6 | null | null | null | 0.73 | 6.68 | 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":46277,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46278,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46279,"numValue":6.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4628... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,370 | train | mutant | 5,907 | 117 | 6,477 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174M | I174M | 1 | 1 | 0 | 0 | 174 | I | M | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 12,751 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92M | null | null | 3.8 | 1.6 | null | null | null | 0.53 | 7.09 | 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":46282,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46283,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46284,"numValue":7.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46285,"numValue":0.53,... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,371 | train | mutant | 5,908 | 117 | 6,478 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174V | I174V | 1 | 1 | 0 | 0 | 174 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 12,752 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92V | null | null | 5 | 0.4 | null | null | null | 0.75 | 6.68 | 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":46287,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46288,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46289,"numValue":6.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4629... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,372 | train | mutant | 5,908 | 117 | 6,478 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174V | I174V | 1 | 1 | 0 | 0 | 174 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 13,444 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92V | null | null | 4.98 | 0.5 | null | null | null | 0.7 | 1.01 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | 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":49567,"numValue":4.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49568,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49569,"numValue":1.01,"references":[],"strValue":n... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,373 | train | mutant | 6,216 | 117 | 6,810 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174E | I174E | 1 | 1 | 0 | 0 | 174 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 13,235 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I92E | null | null | 3.9 | 5.6 | null | null | null | 0.8 | 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":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":48557,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48558,"numValue":5.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48559,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48560,"numValue":0.8,"references":[],"str... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,374 | train | mutant | 6,216 | 117 | 6,810 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174E | I174E | 1 | 1 | 0 | 0 | 174 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 13,236 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I92E | null | null | 5.9 | 5.8 | null | null | null | 1 | 5.9 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48562,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48563,"numValue":5.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48564,"numValue":5.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48565,"numValue":1.0,"references":[],"str... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7376 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,376 | train | mutant | 6,216 | 117 | 6,810 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174E | I174E | 1 | 1 | 0 | 0 | 174 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 13,238 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I92E | null | null | 2.7 | 9.2 | null | null | null | 0.4 | 6.4 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48572,"numValue":2.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48573,"numValue":9.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48574,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48575,"numValue":0.4,"references":[],"str... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,377 | train | mutant | 6,216 | 117 | 6,810 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174E | I174E | 1 | 1 | 0 | 0 | 174 | I | E | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 13,239 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:I92E | null | null | 1.4 | 10.1 | null | null | null | 0.2 | 6.7 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":9.0,"strValue":null,"type":"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":48577,"numValue":1.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48578,"numValue":10.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48579,"numValue":6.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48580,"numValue":0.2,"references":[],"st... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7378 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,378 | train | mutant | 6,311 | 117 | 6,911 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174A | I174A | 1 | 1 | 0 | 0 | 174 | I | A | 8 | CONSERVATION | 1STN | 140 | null | 174 | A | E | true | false | 0.940597 | 9.30375 | 13,445 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92A | null | null | 1.48 | 4 | null | null | null | 0.1 | 1.18 | 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":49572,"numValue":1.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49573,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49574,"numValue":1.18,"references":[],"strValue":n... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,379 | train | mutant | 8,108 | 117 | 8,835 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174L|V181I | I174L|V181I | 2 | 2 | 0 | 0 | 174 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 174|181 | A | E|H | true | false | 0.73904 | 7.983304 | 17,260 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92L 1STN_A:V99I | null | null | 4.5 | 0.9 | null | null | null | 0.67 | 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":63704,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63705,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63706,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63707,"numValue":0.67,"references":[],"s... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,380 | train | mutant | 8,109 | 117 | 8,836 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174L|V181L | I174L|V181L | 2 | 2 | 0 | 0 | 174 | I | L | 8 | CONSERVATION | 1STN | 140 | null | 174|181 | A | E|H | true | false | 0.73904 | 7.983304 | 17,261 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92L 1STN_A:V99L | null | null | 4.1 | 1.3 | null | null | null | 0.63 | 0.96 | 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":63709,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63710,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63711,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63712,"numValue":0.63,"references":[],"s... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7381 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,381 | train | mutant | 8,110 | 117 | 8,837 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174V|V181I | I174V|V181I | 2 | 2 | 0 | 0 | 174 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 174|181 | A | E|H | true | false | 0.73904 | 7.983304 | 17,262 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92V 1STN_A:V99I | null | null | 4.7 | 0.7 | null | null | null | 0.73 | 0.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | ION|ION_CONC|_PDB_CHAIN_MUTATION|PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"100 mM","type":"ION_CONC"},{"numValue":null,"strValue":"1STN_A:I92V 1STN_A:V99I","type":"_PDB_CHAIN_MUTATION"},{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue... | [{"datasets":[],"id":63714,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63715,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63716,"numValue":0.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63717,"numValue":0.73,"references":[],"s... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,382 | train | mutant | 8,111 | 117 | 8,838 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I174V|V181L | I174V|V181L | 2 | 2 | 0 | 0 | 174 | I | V | 8 | CONSERVATION | 1STN | 140 | null | 174|181 | A | E|H | true | false | 0.73904 | 7.983304 | 17,263 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I92V 1STN_A:V99L | null | null | 4.5 | 0.9 | null | null | null | 0.67 | 1 | 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":63719,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":63720,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":63721,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":63722,"numValue":0.67,"references":[],"st... | [{"id":7944,"numValue":8.0,"position":174,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,384 | train | mutant | 1,234 | 117 | 1,384 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y175F | Y175F | 1 | 1 | 0 | 0 | 175 | Y | F | 7 | CONSERVATION | 1STN | 140 | null | 175 | A | E | true | false | 17.088515 | 8.7275 | 2,492 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:Y93F | 46.4 | -6.6 | null | null | null | null | 70 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9178,"numValue":46.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv"],"id":9179,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9180,"numValue":70.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["Broom_S605.csv","PoPMuSiC-2.... | [{"id":7945,"numValue":7.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,385 | train | mutant | 1,234 | 117 | 1,384 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y175F | Y175F | 1 | 1 | 0 | 0 | 175 | Y | F | 7 | CONSERVATION | 1STN | 140 | null | 175 | A | E | true | false | 17.088515 | 8.7275 | 13,500 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y93F | null | null | 3.6 | 2 | null | null | null | 0.59 | 0.92 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49846,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49847,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49848,"numValue":0.92,"references":[],"strValue":nu... | [{"id":7945,"numValue":7.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7386 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,386 | train | mutant | 6,340 | 117 | 6,960 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y175L | Y175L | 1 | 1 | 0 | 0 | 175 | Y | L | 7 | CONSERVATION | 1STN | 140 | null | 175 | A | E | true | false | 17.088515 | 8.7275 | 13,507 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:Y93L | null | null | 1.1 | 4.5 | null | null | null | 0.15 | 1.07 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49878,"numValue":1.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49879,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49880,"numValue":1.07,"references":[],"strValue":nu... | [{"id":7945,"numValue":7.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,387 | train | mutant | 7,977 | 117 | 8,701 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y175W|W222A | Y175W|W222A | 2 | 2 | 0 | 0 | 175 | Y | W | 7 | CONSERVATION | 1STN | 140 | null | 175|222 | A | E|G | true | false | 37.381393 | 15.494464 | 17,070 | ProTherm | 5 | Fluorescence | GdnHCl | Phosphate | 25 | 1STN_A:Y93W 1STN_A:W140A | null | null | null | null | null | null | null | 0.64 | null | null | null | null | null | null | null | null | Unknown | CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 687 | ARTICLE | The role of tryptophan in staphylococcal nuclease stability. | 2,010 | 10.1016/j.bpc.2010.07.001 | 20688426 | Biophys Chem;151;170-7 | 7 | Hu Hong-Yu|Wu Ming-Chya|Fang Huey-Jen|Forrest Michael D|Hu Chin-Kun|Tsong Tian Yow|Chen Hueih Min | [{"numValue":5.0,"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":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1STN_A:Y93W 1S... | [{"datasets":[],"id":62827,"numValue":0.64,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62828,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7945,"numValue":7.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7388 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,388 | train | mutant | 7,977 | 117 | 8,701 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y175W|W222A | Y175W|W222A | 2 | 2 | 0 | 0 | 175 | Y | W | 7 | CONSERVATION | 1STN | 140 | null | 175|222 | A | E|G | true | false | 37.381393 | 15.494464 | 17,072 | ProTherm | 5 | CD | GdnHCl | Phosphate | 25 | 1STN_A:Y93W 1STN_A:W140A | null | null | null | null | null | null | null | 0.5 | null | null | null | null | null | null | null | null | Unknown | CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 687 | ARTICLE | The role of tryptophan in staphylococcal nuclease stability. | 2,010 | 10.1016/j.bpc.2010.07.001 | 20688426 | Biophys Chem;151;170-7 | 7 | Hu Hong-Yu|Wu Ming-Chya|Fang Huey-Jen|Forrest Michael D|Hu Chin-Kun|Tsong Tian Yow|Chen Hueih Min | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1STN_A:Y93W 1STN_A:W140A... | [{"datasets":[],"id":62831,"numValue":0.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62832,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7945,"numValue":7.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,389 | train | mutant | 7,977 | 117 | 8,701 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Y175W|W222A | Y175W|W222A | 2 | 2 | 0 | 0 | 175 | Y | W | 7 | CONSERVATION | 1STN | 140 | null | 175|222 | A | E|G | true | false | 37.381393 | 15.494464 | 17,074 | ProTherm | 8.8 | Fluorescence | Activity | Tris-HCl | 25 mM | 25 | Calcium chloride | 10 mM | 1STN_A:Y93W 1STN_A:W140A | null | null | null | null | null | null | null | 0.09 | null | null | null | null | null | null | null | null | Unknown | CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 687 | ARTICLE | The role of tryptophan in staphylococcal nuclease stability. | 2,010 | 10.1016/j.bpc.2010.07.001 | 20688426 | Biophys Chem;151;170-7 | 7 | Hu Hong-Yu|Wu Ming-Chya|Fang Huey-Jen|Forrest Michael D|Hu Chin-Kun|Tsong Tian Yow|Chen Hueih Min | [{"numValue":8.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Activity","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type"... | [{"datasets":[],"id":62835,"numValue":0.09,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":62836,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7945,"numValue":7.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,390 | train | mutant | 6,099 | 117 | 6,687 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A176G | A176G | 1 | 1 | 0 | 0 | 176 | A | G | 6 | CONSERVATION | 1STN | 140 | null | 176 | A | E | true | false | 3.995289 | 8.76 | 13,010 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A94G | null | null | 3.1 | 2.4 | null | null | null | 0.41 | 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 | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47521,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47522,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47523,"numValue":1.12,"references":[],"strValue":nu... | [{"id":7946,"numValue":6.0,"position":176,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7391 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,391 | train | mutant | 6,100 | 117 | 6,688 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A176V | A176V | 1 | 1 | 0 | 0 | 176 | A | V | 6 | CONSERVATION | 1STN | 140 | null | 176 | A | E | true | false | 3.995289 | 8.76 | 13,011 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A94V | null | null | 4.2 | 1.3 | null | null | null | 0.66 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47526,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47527,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47528,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47529,"numValue":0.66,... | [{"id":7946,"numValue":6.0,"position":176,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,392 | train | mutant | 5,952 | 117 | 6,522 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D177A | D177A | 1 | 1 | 0 | 0 | 177 | D | A | 7 | CONSERVATION | 1STN | 140 | null | 177 | A | T | true | false | 60.52802 | 12.6975 | 12,822 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D95A | null | null | 2.3 | 3.3 | null | null | null | 0.28 | 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 | 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":46626,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46627,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46628,"numValue":1.13,"references":[],"strValue":nu... | [{"id":7947,"numValue":7.0,"position":177,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,393 | train | mutant | 5,952 | 117 | 6,522 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D177A | D177A | 1 | 1 | 0 | 0 | 177 | D | A | 7 | CONSERVATION | 1STN | 140 | null | 177 | A | T | true | false | 60.52802 | 12.6975 | 13,145 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D95A | null | null | -3.6 | 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":48119,"numValue":-3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48120,"numValue":1.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48121,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7947,"numValue":7.0,"position":177,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7394 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,394 | train | mutant | 5,952 | 117 | 6,522 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D177A | D177A | 1 | 1 | 0 | 0 | 177 | D | A | 7 | CONSERVATION | 1STN | 140 | null | 177 | A | T | true | false | 60.52802 | 12.6975 | 13,552 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D95A | null | null | 2.1 | 3.3 | null | null | null | 0.28 | 1.13 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | 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":50090,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":50091,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50092,"numValue":1.13,"references":[],"strValue":nu... | [{"id":7947,"numValue":7.0,"position":177,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7396 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,396 | train | mutant | 5,953 | 117 | 6,523 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D177G | D177G | 1 | 1 | 0 | 0 | 177 | D | G | 7 | CONSERVATION | 1STN | 140 | null | 177 | A | T | true | false | 60.52802 | 12.6975 | 13,146 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D95G | null | null | -3.1 | null | null | null | null | null | 1.03 | 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":48122,"numValue":-3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48123,"numValue":1.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48124,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7947,"numValue":7.0,"position":177,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7397 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,397 | train | mutant | 5,953 | 117 | 6,523 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D177G | D177G | 1 | 1 | 0 | 0 | 177 | D | G | 7 | CONSERVATION | 1STN | 140 | null | 177 | A | T | true | false | 60.52802 | 12.6975 | 13,553 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D95G | null | null | 2.7 | 2.7 | null | null | null | 0.37 | 1.11 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | 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":50095,"numValue":2.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":50096,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50097,"numValue":1.11,"references":[],"strValue":nu... | [{"id":7947,"numValue":7.0,"position":177,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7398 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,398 | train | mutant | 6,252 | 117 | 6,847 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D177F | D177F | 1 | 1 | 0 | 0 | 177 | D | F | 7 | CONSERVATION | 1STN | 140 | null | 177 | A | T | true | false | 60.52802 | 12.6975 | 13,357 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:D95F | null | null | 0.2 | 5.3 | null | null | null | 0.06 | 0.59 | 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":49140,"numValue":0.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49141,"numValue":5.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49142,"numValue":0.59,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49143,"numValue":0.06,... | [{"id":7947,"numValue":7.0,"position":177,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,399 | train | mutant | 1,289 | 117 | 1,439 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G178F | G178F | 1 | 1 | 0 | 0 | 178 | G | F | 7 | CONSERVATION | 1STN | 140 | null | 178 | A | T | true | false | 53.93805 | 12.9525 | 2,453 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:G96F | 42 | -10.7 | null | null | null | null | 73 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":9022,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9023,"numValue":-10.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9024,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9025,"numValue":null,"references":[],... | [{"id":7948,"numValue":7.0,"position":178,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,401 | train | mutant | 1,289 | 117 | 1,439 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G178F | G178F | 1 | 1 | 0 | 0 | 178 | G | F | 7 | CONSERVATION | 1STN | 140 | null | 178 | A | T | true | false | 53.93805 | 12.9525 | 13,358 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G96F | null | null | 2.5 | 3 | null | null | null | 0.51 | 0.75 | 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":49145,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49146,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49147,"numValue":0.75,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49148,"numValue":0.51,... | [{"id":7948,"numValue":7.0,"position":178,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,402 | train | mutant | 6,137 | 117 | 6,725 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G178A | G178A | 1 | 1 | 0 | 0 | 178 | G | A | 7 | CONSERVATION | 1STN | 140 | null | 178 | A | T | true | false | 53.93805 | 12.9525 | 13,050 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G96A | null | null | 3.7 | 1.8 | null | null | null | 0.53 | 1.02 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47721,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47722,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47723,"numValue":1.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47724,"numValue":0.53,... | [{"id":7948,"numValue":7.0,"position":178,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,403 | train | mutant | 6,137 | 117 | 6,725 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G178A | G178A | 1 | 1 | 0 | 0 | 178 | G | A | 7 | CONSERVATION | 1STN | 140 | null | 178 | A | T | true | false | 53.93805 | 12.9525 | 13,563 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G96A | null | null | 3.7 | 1.7 | null | null | null | 0.53 | 1.02 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50145,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50146,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50147,"numValue":1.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50148,"numValue":0.53,... | [{"id":7948,"numValue":7.0,"position":178,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7404 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,404 | train | mutant | 6,138 | 117 | 6,726 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | G178V | G178V | 1 | 1 | 0 | 0 | 178 | G | V | 7 | CONSERVATION | 1STN | 140 | null | 178 | A | T | true | false | 53.93805 | 12.9525 | 13,051 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:G96V | null | null | 1.8 | 3.7 | null | null | null | 0.25 | 1.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47726,"numValue":1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47727,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47728,"numValue":1.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47729,"numValue":0.25,... | [{"id":7948,"numValue":7.0,"position":178,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7406 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,406 | train | mutant | 6,011 | 117 | 6,581 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K179G | K179G | 1 | 1 | 0 | 0 | 179 | K | G | 4 | CONSERVATION | 1STN | 140 | null | 179 | A | E | true | false | 130.283108 | 27.706666 | 12,885 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K97G | null | null | 3.9 | 1.7 | null | null | null | 0.51 | 1.09 | 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":46941,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":46942,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46943,"numValue":1.09,"references":[],"strValue":nu... | [{"id":7949,"numValue":4.0,"position":179,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,407 | train | mutant | 6,068 | 117 | 6,653 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K179E | K179E | 1 | 1 | 0 | 0 | 179 | K | E | 4 | CONSERVATION | 1STN | 140 | null | 179 | A | E | true | false | 130.283108 | 27.706666 | 12,945 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1STN_A:K97E | null | null | 4.8 | 0.6 | null | null | null | 0.77 | 6.2 | 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":47241,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47242,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47243,"numValue":6.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47244... | [{"id":7949,"numValue":4.0,"position":179,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7409 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,409 | train | mutant | 6,253 | 117 | 6,848 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K179F | K179F | 1 | 1 | 0 | 0 | 179 | K | F | 4 | CONSERVATION | 1STN | 140 | null | 179 | A | E | true | false | 130.283108 | 27.706666 | 13,359 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K97F | null | null | 4.8 | 0.7 | null | null | null | 0.76 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 845 | ARTICLE | Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. | 1,998 | 10.1021/bi9725069 | 9578580 | Biochemistry;37;6939-48 | 4 | Stites W E|Schwehm J M|Kristyanne E S|Biggers C C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49150,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49151,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49152,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49153,"numValue":0.76,... | [{"id":7949,"numValue":4.0,"position":179,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,410 | train | mutant | 5,881 | 117 | 6,451 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | M180I | M180I | 1 | 1 | 0 | 0 | 180 | M | I | 7 | CONSERVATION | 1STN | 140 | null | 180 | A | E | false | false | 20.469708 | 9.30125 | 12,723 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:M98I | null | null | 1 | 4.4 | null | null | null | 0.15 | 1.02 | 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 | 820 | ARTICLE | Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins. | 2,001 | 10.1093/protein/14.5.343 | 11438757 | Protein Eng;14;343-7 | 4 | Stites W E|Spencer D S|Kim Y H|Berry A H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46142,"numValue":1.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46143,"numValue":4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46144,"numValue":1.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46145,"numValue":0.15,... | [{"id":7950,"numValue":7.0,"position":180,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7411 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,411 | train | mutant | 6,320 | 117 | 6,920 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | M180A | M180A | 1 | 1 | 0 | 0 | 180 | M | A | 7 | CONSERVATION | 1STN | 140 | null | 180 | A | E | false | false | 20.469708 | 9.30125 | 13,455 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:M98A | null | null | 0.88 | 4.6 | null | null | null | 0.1 | 0.75 | 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":49622,"numValue":0.88,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49623,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49624,"numValue":0.75,"references":[],"strValue":n... | [{"id":7950,"numValue":7.0,"position":180,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7413 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,413 | train | mutant | 1,222 | 117 | 1,372 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181T | V181T | 1 | 1 | 0 | 0 | 181 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 2,385 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V99T | 37.5 | -15.2 | null | null | null | null | 68 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv"],"id":8750,"numValue":37.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv"],"id":8751,"numValue":-15.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv"],"... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,414 | train | mutant | 1,222 | 117 | 1,372 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181T | V181T | 1 | 1 | 0 | 0 | 181 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 2,480 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V99T | 39.1 | -13.8 | null | null | null | null | 65 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["Broom_S605.csv","EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv"],"id":9130,"numValue":39.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv"]... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,415 | train | mutant | 1,222 | 117 | 1,372 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181T | V181T | 1 | 1 | 0 | 0 | 181 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,483 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V99T | null | null | 2.3 | 3.3 | null | null | null | 0.32 | 1.07 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49761,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49762,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49763,"numValue":1.07,"references":[],"strValue":nu... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,416 | train | mutant | 5,893 | 117 | 6,463 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181I | V181I | 1 | 1 | 0 | 0 | 181 | V | I | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 12,736 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V99I | null | null | 5.2 | 0.2 | null | null | null | 0.81 | 6.4 | 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":46207,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46208,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46209,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46210... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,417 | train | mutant | 5,894 | 117 | 6,464 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181L | V181L | 1 | 1 | 0 | 0 | 181 | V | L | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 12,737 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V99L | null | null | 5.1 | 0.3 | null | null | null | 0.82 | 6.27 | 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":46212,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46213,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46214,"numValue":6.27,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4621... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,418 | train | mutant | 6,217 | 117 | 6,811 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181E | V181E | 1 | 1 | 0 | 0 | 181 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,240 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V99E | null | null | 4.7 | 4.8 | null | null | null | 0.9 | 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":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":48582,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48583,"numValue":4.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48584,"numValue":5.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48585,"numValue":0.9,"references":[],"str... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,419 | train | mutant | 6,217 | 117 | 6,811 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181E | V181E | 1 | 1 | 0 | 0 | 181 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,241 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V99E | null | null | 6.2 | 5.5 | null | null | null | 1.1 | 5.4 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48587,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48588,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48589,"numValue":5.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48590,"numValue":1.1,"references":[],"str... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,421 | train | mutant | 6,217 | 117 | 6,811 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181E | V181E | 1 | 1 | 0 | 0 | 181 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,243 | ProTherm | 7.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V99E | null | null | 3.2 | 8.7 | null | null | null | 0.5 | 6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":7.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48597,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48598,"numValue":8.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48599,"numValue":6.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48600,"numValue":0.5,"references":[],"str... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,422 | train | mutant | 6,217 | 117 | 6,811 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181E | V181E | 1 | 1 | 0 | 0 | 181 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,244 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V99E | null | null | 2.1 | 9.5 | null | null | null | 0.3 | 6.4 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48602,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48603,"numValue":9.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48604,"numValue":6.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48605,"numValue":0.3,"references":[],"str... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,424 | train | mutant | 6,298 | 117 | 6,898 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181G | V181G | 1 | 1 | 0 | 0 | 181 | V | G | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,430 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V99G | null | null | 0.48 | 5 | null | null | null | null | 1.18 | null | null | null | null | null | null | null | yes | DG|DDG|M|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":49498,"numValue":0.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49499,"numValue":5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49500,"numValue":1.18,"references":[],"strValue":n... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,425 | train | mutant | 6,337 | 117 | 6,957 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V181S | V181S | 1 | 1 | 0 | 0 | 181 | V | S | 7 | CONSERVATION | 1STN | 140 | null | 181 | A | H | true | false | 0.537484 | 6.662857 | 13,492 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V99S | null | null | 0.5 | 5.1 | null | null | null | 0.07 | 1.15 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 853 | ARTICLE | Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. | 1,995 | 10.1021/bi00042a029 | 7577991 | Biochemistry;34;13949-60 | 4 | Stites W E|Byrne M P|Manuel R L|Lowe L G | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49806,"numValue":0.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49807,"numValue":5.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49808,"numValue":1.15,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49809,"numValue":0.07,... | [{"id":7951,"numValue":7.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,426 | train | mutant | 6,143 | 117 | 6,731 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182G | N182G | 1 | 1 | 0 | 0 | 182 | N | G | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,056 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:N100G | null | null | 0.4 | 5.1 | null | null | null | 0.09 | 0.71 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47749,"numValue":0.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47750,"numValue":5.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47751,"numValue":0.71,"references":[],"strValue":nu... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,427 | train | mutant | 6,144 | 117 | 6,732 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182A | N182A | 1 | 1 | 0 | 0 | 182 | N | A | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,057 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:N100A | null | null | 0.3 | 5.2 | null | null | null | 0.05 | 0.8 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47754,"numValue":0.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47755,"numValue":5.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47756,"numValue":0.8,"references":[],"strValue":nul... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,428 | train | mutant | 6,218 | 117 | 6,812 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182E | N182E | 1 | 1 | 0 | 0 | 182 | N | E | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,245 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:N100E | null | null | 9.5 | -0.1 | null | null | null | 2 | 4.7 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48607,"numValue":9.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48608,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48609,"numValue":4.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48610,"numValue":2.0,"references":[],"st... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,429 | train | mutant | 6,218 | 117 | 6,812 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182E | N182E | 1 | 1 | 0 | 0 | 182 | N | E | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,246 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:N100E | null | null | 10.6 | 1.2 | null | null | null | 2.1 | 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":48612,"numValue":10.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48613,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48614,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48615,"numValue":2.1,"references":[],"st... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,430 | train | mutant | 6,218 | 117 | 6,812 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182E | N182E | 1 | 1 | 0 | 0 | 182 | N | E | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,247 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:N100E | null | null | 9.3 | 2.4 | null | null | null | 1.9 | 5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48617,"numValue":9.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48618,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48619,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48620,"numValue":1.9,"references":[],"str... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,431 | train | mutant | 6,218 | 117 | 6,812 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182E | N182E | 1 | 1 | 0 | 0 | 182 | N | E | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,248 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:N100E | null | null | 7.4 | 4.4 | null | null | null | 1.4 | 5.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48622,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48623,"numValue":4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48624,"numValue":5.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48625,"numValue":1.4,"references":[],"str... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,432 | train | mutant | 6,218 | 117 | 6,812 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N182E | N182E | 1 | 1 | 0 | 0 | 182 | N | E | 9 | CONSERVATION | 1STN | 140 | null | 182 | A | H | false | false | 0 | 7.07 | 13,249 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:N100E | null | null | 7.1 | 4.5 | null | null | null | 1.3 | 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":48627,"numValue":7.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48628,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48629,"numValue":5.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48630,"numValue":1.3,"references":[],"str... | [{"id":7952,"numValue":9.0,"position":182,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,433 | train | mutant | 1,290 | 117 | 1,440 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E183F | E183F | 1 | 1 | 0 | 0 | 183 | E | F | 6 | CONSERVATION | 1STN | 140 | null | 183 | A | H | false | false | 37.200913 | 13.365555 | 2,454 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E101F | 37.6 | -16.1 | null | null | null | null | 62 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":9026,"numValue":37.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9027,"numValue":-16.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9028,"numValue":62.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9029,"numValue":null,"references":[],... | [{"id":7953,"numValue":6.0,"position":183,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7434 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,434 | train | mutant | 1,290 | 117 | 1,440 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E183F | E183F | 1 | 1 | 0 | 0 | 183 | E | F | 6 | CONSERVATION | 1STN | 140 | null | 183 | A | H | false | false | 37.200913 | 13.365555 | 2,549 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:E101F | 39.7 | -13.3 | null | null | null | null | 56 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":9406,"numValue":39.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9407,"numValue":-13.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9408,"numValue":56.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9409,"numValue":null,"references":[],... | [{"id":7953,"numValue":6.0,"position":183,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,435 | train | mutant | 1,290 | 117 | 1,440 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E183F | E183F | 1 | 1 | 0 | 0 | 183 | E | F | 6 | CONSERVATION | 1STN | 140 | null | 183 | A | H | false | false | 37.200913 | 13.365555 | 13,360 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:E101F | null | null | 2.4 | 3.1 | null | null | null | 0.47 | 0.78 | 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":49155,"numValue":2.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49156,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49157,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49158,"numValue":0.47,... | [{"id":7953,"numValue":6.0,"position":183,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,439 | train | mutant | 6,102 | 117 | 6,690 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A184V | A184V | 1 | 1 | 0 | 0 | 184 | A | V | 4 | CONSERVATION | 1STN | 140 | null | 184 | A | H | true | false | 18.140077 | 8.77 | 13,013 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A102V | null | null | 3.6 | 1.9 | null | null | null | 0.54 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 833 | ARTICLE | Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. | 1,992 | 10.1021/bi00140a005 | 1610820 | Biochemistry;31;5717-28 | 3 | Shortle D|Meeker A K|Green S M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":47536,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":47537,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47538,"numValue":0.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47539,"numValue":0.54,... | [{"id":7954,"numValue":4.0,"position":184,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,440 | train | mutant | 6,254 | 117 | 6,849 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A184F | A184F | 1 | 1 | 0 | 0 | 184 | A | F | 4 | CONSERVATION | 1STN | 140 | null | 184 | A | H | true | false | 18.140077 | 8.77 | 13,361 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:A102F | null | null | 3.6 | 1.9 | null | null | null | 0.6 | 0.91 | 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":49160,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":49161,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49162,"numValue":0.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49163,"numValue":0.6,"... | [{"id":7954,"numValue":4.0,"position":184,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,441 | train | mutant | 5,925 | 117 | 6,495 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185I | L185I | 1 | 1 | 0 | 0 | 185 | L | I | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 12,769 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L103I | null | null | 4.3 | 1.1 | null | null | null | 0.65 | 6.68 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46372,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46373,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46374,"numValue":6.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46375,"numValue":0.65,... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,442 | train | mutant | 5,926 | 117 | 6,496 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185V | L185V | 1 | 1 | 0 | 0 | 185 | L | V | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 12,770 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L103V | null | null | 3.4 | 2 | null | null | null | 0.5 | 6.82 | 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":46377,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46378,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46379,"numValue":6.82,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46380,"numValue":0.5,"... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,443 | train | mutant | 6,199 | 117 | 6,793 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185A | L185A | 1 | 1 | 0 | 0 | 185 | L | A | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,147 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L103A | null | null | -4.6 | 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":48125,"numValue":-4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48126,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48127,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,444 | train | mutant | 6,199 | 117 | 6,793 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185A | L185A | 1 | 1 | 0 | 0 | 185 | L | A | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,417 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L103A | null | null | 0.88 | 4.6 | null | null | null | 0.1 | 0.96 | 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":49433,"numValue":0.88,"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":49434,"numValue":4.6,"references":[],"strValue":null,"... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,445 | train | mutant | 6,219 | 117 | 6,813 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185E | L185E | 1 | 1 | 0 | 0 | 185 | L | E | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,250 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L103E | null | null | 5.7 | 3.8 | null | null | null | 1.2 | 4.8 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":3.9,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48632,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48633,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48634,"numValue":4.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48635,"numValue":1.2,"references":[],"str... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,446 | train | mutant | 6,219 | 117 | 6,813 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185E | L185E | 1 | 1 | 0 | 0 | 185 | L | E | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,251 | ProTherm | 5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L103E | null | null | 7.6 | 4.2 | null | null | null | 1.4 | 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":48637,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48638,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48639,"numValue":5.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48640,"numValue":1.4,"references":[],"str... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,447 | train | mutant | 6,219 | 117 | 6,813 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185E | L185E | 1 | 1 | 0 | 0 | 185 | L | E | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,252 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L103E | null | null | 6.6 | 5.1 | null | null | null | 1.2 | 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":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":48642,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48643,"numValue":5.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48644,"numValue":5.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48645,"numValue":1.2,"references":[],"str... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,448 | train | mutant | 6,219 | 117 | 6,813 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185E | L185E | 1 | 1 | 0 | 0 | 185 | L | E | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,253 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L103E | null | null | 4.7 | 7.2 | null | null | null | 0.8 | 5.9 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48647,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48648,"numValue":7.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48649,"numValue":5.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48650,"numValue":0.8,"references":[],"str... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7449 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,449 | train | mutant | 6,219 | 117 | 6,813 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L185E | L185E | 1 | 1 | 0 | 0 | 185 | L | E | 8 | CONSERVATION | 1STN | 140 | null | 185 | A | H | false | false | 0 | 9.2925 | 13,254 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:L103E | null | null | 3.4 | 8.2 | null | null | null | 0.6 | 6.1 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48652,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48653,"numValue":8.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48654,"numValue":6.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48655,"numValue":0.6,"references":[],"str... | [{"id":7955,"numValue":8.0,"position":185,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7450 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,450 | train | mutant | 1,223 | 117 | 1,373 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186T | V186T | 1 | 1 | 0 | 0 | 186 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 2,386 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V104T | 42.4 | -10.3 | null | null | null | null | 65 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":[],"id":8754,"numValue":42.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8755,"numValue":-10.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":8756,"numValue":65.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8757,"numValue":null,"references":[],... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7451 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,451 | train | mutant | 1,223 | 117 | 1,373 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186T | V186T | 1 | 1 | 0 | 0 | 186 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 2,481 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:V104T | 43.5 | -9.5 | null | null | null | null | 65 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":["Broom_S605.csv","EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":9134,"numValue":43.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,452 | train | mutant | 1,223 | 117 | 1,373 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186T | V186T | 1 | 1 | 0 | 0 | 186 | V | T | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,484 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V104T | null | null | 3.1 | 2.5 | null | null | null | 0.47 | 0.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49766,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49767,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49768,"numValue":0.98,"references":[],"strValue":nu... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,453 | train | mutant | 5,895 | 117 | 6,465 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186I | V186I | 1 | 1 | 0 | 0 | 186 | V | I | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 12,738 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V104I | null | null | 5.6 | -0.2 | null | null | null | 0.87 | 6.41 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 821 | ARTICLE | Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. | 2,001 | 10.1021/bi011267t | 11705391 | Biochemistry;40;13998-4003 | 6 | Chen J|Stites W E|Spencer D S|Byrne M P|Holder J B|Bennett A F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":46217,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46218,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46219,"numValue":6.41,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":462... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7454 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,454 | train | mutant | 5,896 | 117 | 6,466 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186L | V186L | 1 | 1 | 0 | 0 | 186 | V | L | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 12,739 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:V104L | null | null | 4.6 | 0.8 | null | null | null | 0.71 | 6.48 | 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":46222,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46223,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46224,"numValue":6.48,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46225,"numValue":0.71,... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,455 | train | mutant | 6,220 | 117 | 6,814 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186E | V186E | 1 | 1 | 0 | 0 | 186 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,255 | ProTherm | 3.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V104E | null | null | 7.5 | 2 | 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":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":48657,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48658,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48659,"numValue":5.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48660,"numValue":1.5,"references":[],"str... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,456 | train | mutant | 6,220 | 117 | 6,814 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186E | V186E | 1 | 1 | 0 | 0 | 186 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,256 | ProTherm | 4.9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V104E | null | null | 8.9 | 2.8 | null | null | null | 1.7 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48662,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48663,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48664,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48665,"numValue":1.7,"references":[],"str... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,457 | train | mutant | 6,220 | 117 | 6,814 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186E | V186E | 1 | 1 | 0 | 0 | 186 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,257 | ProTherm | 5.5 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V104E | null | null | 8.5 | 3.2 | null | null | null | 1.6 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":48667,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48668,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48669,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48670,"numValue":1.6,"references":[],"str... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,458 | train | mutant | 6,220 | 117 | 6,814 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186E | V186E | 1 | 1 | 0 | 0 | 186 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,258 | ProTherm | 6 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V104E | null | null | 7.6 | 4.1 | null | null | null | 1.4 | 5.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48672,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48673,"numValue":4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48674,"numValue":5.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48675,"numValue":1.4,"references":[],"str... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,459 | train | mutant | 6,220 | 117 | 6,814 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186E | V186E | 1 | 1 | 0 | 0 | 186 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,259 | ProTherm | 8 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V104E | null | null | 5.4 | 6.5 | null | null | null | 1 | 5.7 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48677,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48678,"numValue":6.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48679,"numValue":5.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48680,"numValue":1.0,"references":[],"str... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,460 | train | mutant | 6,220 | 117 | 6,814 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | V186E | V186E | 1 | 1 | 0 | 0 | 186 | V | E | 7 | CONSERVATION | 1STN | 140 | null | 186 | A | H | false | false | 0 | 10.09 | 13,260 | ProTherm | 9 | Fluorescence | GdnHCl | HEPES | 10 mM | 20 | NaCl | 100 mM | 1STN_A:V104E | null | null | 4.2 | 7.4 | null | null | null | 0.7 | 5.9 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 840 | ARTICLE | Charges in the hydrophobic interior of proteins. | 2,010 | 10.1073/pnas.1004213107 | 20798341 | Proc Natl Acad Sci U S A;107;16096-100 | 5 | Isom Daniel G|Garc?a-Moreno E Bertrand|Casta?eda Carlos A|Cannon Brian R|Velu Priya D | [{"numValue":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":48682,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":48683,"numValue":7.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":48684,"numValue":5.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":48685,"numValue":0.7,"references":[],"str... | [{"id":7956,"numValue":7.0,"position":186,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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