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:7687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,687 | train | mutant | 6,022 | 117 | 6,592 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | K218G | K218G | 1 | 1 | 0 | 0 | 218 | K | G | 4 | CONSERVATION | 1STN | 140 | null | 218 | A | T | false | false | 140.289445 | 34.795556 | 13,551 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:K136G | null | null | 5.5 | -0.1 | null | null | null | 0.82 | 1.01 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50085,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50086,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50087,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{... | [{"id":7988,"numValue":4.0,"position":218,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,689 | train | mutant | 1,607 | 117 | 1,807 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L219A | L219A | 1 | 1 | 0 | 0 | 219 | L | A | 3 | CONSERVATION | 1STN | 140 | null | 219 | A | L | false | false | 52.404668 | 18.25375 | 13,419 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L137A | null | null | 3.18 | 2.3 | null | null | null | 0.5 | 0.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49443,"numValue":3.18,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49444,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49445,"numValue":0.95,"references":[],"strValue":n... | [{"id":7989,"numValue":3.0,"position":219,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,690 | train | mutant | 5,931 | 117 | 6,501 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L219I | L219I | 1 | 1 | 0 | 0 | 219 | L | I | 3 | CONSERVATION | 1STN | 140 | null | 219 | A | L | false | false | 52.404668 | 18.25375 | 12,775 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L137I | null | null | 4.6 | 0.8 | null | null | null | 0.71 | 6.5 | 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":46402,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46403,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46404,"numValue":6.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46405,"numValue":0.71,"... | [{"id":7989,"numValue":3.0,"position":219,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,691 | train | mutant | 5,932 | 117 | 6,502 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | L219V | L219V | 1 | 1 | 0 | 0 | 219 | L | V | 3 | CONSERVATION | 1STN | 140 | null | 219 | A | L | false | false | 52.404668 | 18.25375 | 12,776 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:L137V | null | null | 4 | 1.4 | null | null | null | 0.6 | 6.58 | 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":46407,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":46408,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46409,"numValue":6.58,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46410,"numValue":0.6,"... | [{"id":7989,"numValue":3.0,"position":219,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,693 | train | mutant | 6,149 | 117 | 6,737 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N220G | N220G | 1 | 1 | 0 | 0 | 220 | N | G | 8 | CONSERVATION | 1STN | 140 | null | 220 | A | G | false | false | 47.518976 | 20.82875 | 13,062 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:N138G | null | null | 5.6 | -0.1 | null | null | null | 0.95 | 0.87 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|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":47779,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47780,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47781,"numValue":0.87,"reference... | [{"id":7990,"numValue":8.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,694 | train | mutant | 6,149 | 117 | 6,737 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N220G | N220G | 1 | 1 | 0 | 0 | 220 | N | G | 8 | CONSERVATION | 1STN | 140 | null | 220 | A | G | false | false | 47.518976 | 20.82875 | 13,587 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:N138G | null | null | 5.6 | -0.2 | null | null | null | 0.95 | 0.87 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 856 | ARTICLE | Evidence for strained interactions between side-chains and the polypeptide backbone. | 1,994 | 10.1016/s0022-2836(05)80008-7 | 8289248 | J Mol Biol;235;27-32 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":50265,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":50266,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50267,"numValue":0.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":502... | [{"id":7990,"numValue":8.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,695 | train | mutant | 6,150 | 117 | 6,738 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N220A | N220A | 1 | 1 | 0 | 0 | 220 | N | A | 8 | CONSERVATION | 1STN | 140 | null | 220 | A | G | false | false | 47.518976 | 20.82875 | 13,063 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:N138A | null | null | 4.4 | 1.1 | null | null | null | 0.67 | 0.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47784,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47785,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47786,"numValue":0.97,"references":[],"strValue":nu... | [{"id":7990,"numValue":8.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,696 | train | mutant | 6,150 | 117 | 6,738 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | N220A | N220A | 1 | 1 | 0 | 0 | 220 | N | A | 8 | CONSERVATION | 1STN | 140 | null | 220 | A | G | false | false | 47.518976 | 20.82875 | 13,586 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:N138A | null | null | 4.4 | 1 | null | null | null | 0.67 | 0.97 | 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":50260,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":50261,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":50262,"numValue":0.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":50263,"numValue":0.67,... | [{"id":7990,"numValue":8.0,"position":220,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,697 | train | mutant | 5,909 | 117 | 6,479 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I221L | I221L | 1 | 1 | 0 | 0 | 221 | I | L | 9 | CONSERVATION | 1STN | 140 | null | 221 | A | G | true | false | 45.466614 | 25.39625 | 12,753 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I139L | null | null | 5.3 | 0.1 | null | null | null | 0.81 | 6.55 | 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":46292,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46293,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46294,"numValue":6.55,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4629... | [{"id":7991,"numValue":9.0,"position":221,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,698 | train | mutant | 5,910 | 117 | 6,480 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I221M | I221M | 1 | 1 | 0 | 0 | 221 | I | M | 9 | CONSERVATION | 1STN | 140 | null | 221 | A | G | true | false | 45.466614 | 25.39625 | 12,754 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I139M | null | null | 5 | 0.4 | null | null | null | 0.76 | 6.66 | 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":46297,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":46298,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46299,"numValue":6.66,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":4630... | [{"id":7991,"numValue":9.0,"position":221,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,699 | train | mutant | 6,312 | 117 | 6,912 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I221V | I221V | 1 | 1 | 0 | 0 | 221 | I | V | 9 | CONSERVATION | 1STN | 140 | null | 221 | A | G | true | false | 45.466614 | 25.39625 | 13,446 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I139V | null | null | 3.98 | 1.5 | null | null | null | 0.6 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 850 | ARTICLE | Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. | 1,990 | 10.1021/bi00487a007 | 2261461 | Biochemistry;29;8033-41 | 3 | Shortle D|Stites W E|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":49577,"numValue":3.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49578,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49579,"numValue":0.94,"references":[],"strValue":n... | [{"id":7991,"numValue":9.0,"position":221,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,700 | train | mutant | 6,313 | 117 | 6,913 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I221A | I221A | 1 | 1 | 0 | 0 | 221 | I | A | 9 | CONSERVATION | 1STN | 140 | null | 221 | A | G | true | false | 45.466614 | 25.39625 | 13,447 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I139A | null | null | 1.98 | 3.5 | null | null | null | 0.3 | 0.85 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":49582,"numValue":1.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49583,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49584,"numValue":0.85,"references":[],"strValue":n... | [{"id":7991,"numValue":9.0,"position":221,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,701 | train | mutant | 6,314 | 117 | 6,914 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | I221G | I221G | 1 | 1 | 0 | 0 | 221 | I | G | 9 | CONSERVATION | 1STN | 140 | null | 221 | A | G | true | false | 45.466614 | 25.39625 | 13,448 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:I139G | null | null | 1.08 | 4.4 | null | null | null | 0.2 | 0.73 | 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":49587,"numValue":1.08,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":49588,"numValue":4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49589,"numValue":0.73,"references":[],"strValue":n... | [{"id":7991,"numValue":9.0,"position":221,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,703 | train | mutant | 859 | 117 | 966 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222H | W222H | 1 | 1 | 0 | 0 | 222 | W | H | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 1,803 | ProTherm | 7 | CD | Thermal | MOPS | 10 mM | null | 1STN_A:W140H | 41.8 | -8.9 | null | null | null | null | 59.03 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1925.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 191 | ARTICLE | Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease. | 2,005 | 10.1002/prot.20333 | 15573380 | Proteins;58;271-7 | 4 | Hirano Satoshi|Yamazaki Yoichi|Kamikubo Hironari|Kataoka Mikio | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1STN_A:W140H","type":"_PDB_CH... | [{"datasets":["EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6702,"numValue":41.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUT... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,704 | train | mutant | 859 | 117 | 966 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222H | W222H | 1 | 1 | 0 | 0 | 222 | W | H | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 12,973 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | 20 | NaCl | 50 mM | 1STN_A:W140H | null | null | 5.7 | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BU... | [{"datasets":[],"id":47371,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":47372,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47373,"numValue":null,"references":[],"strValue":"yes","type... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,705 | train | mutant | 860 | 117 | 967 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222F | W222F | 1 | 1 | 0 | 0 | 222 | W | F | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 1,488 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | null | NaCl | 50 mM | 1STN_A:W140F | 56.9 | null | null | null | null | null | 81 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":5450,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5451,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5452,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,706 | train | mutant | 860 | 117 | 967 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222F | W222F | 1 | 1 | 0 | 0 | 222 | W | F | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 1,801 | ProTherm | 7 | CD | Thermal | MOPS | 10 mM | null | 1STN_A:W140F | 39.1 | -11.6 | null | null | null | null | 47.8 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 191 | ARTICLE | Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease. | 2,005 | 10.1002/prot.20333 | 15573380 | Proteins;58;271-7 | 4 | Hirano Satoshi|Yamazaki Yoichi|Kamikubo Hironari|Kataoka Mikio | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1STN_A:W140F","type":"_PDB_CH... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6694,"numValue":39.1,"references":[],"strValue":... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,707 | train | mutant | 860 | 117 | 967 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222F | W222F | 1 | 1 | 0 | 0 | 222 | W | F | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 12,974 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | 20 | NaCl | 50 mM | 1STN_A:W140F | null | null | 5.5 | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BU... | [{"datasets":[],"id":47374,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":47375,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47376,"numValue":null,"references":[],"strValue":"yes","type... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,708 | train | mutant | 861 | 117 | 968 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222Y | W222Y | 1 | 1 | 0 | 0 | 222 | W | Y | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 1,489 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | null | NaCl | 50 mM | 1STN_A:W140Y | 56.4 | null | null | null | null | null | 76.8 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":5453,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5454,"numValue":76.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5455,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,709 | train | mutant | 861 | 117 | 968 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222Y | W222Y | 1 | 1 | 0 | 0 | 222 | W | Y | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 1,802 | ProTherm | 7 | CD | Thermal | MOPS | 10 mM | null | 1STN_A:W140Y | 38.6 | -12.1 | null | null | null | null | 49 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 191 | ARTICLE | Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease. | 2,005 | 10.1002/prot.20333 | 15573380 | Proteins;58;271-7 | 4 | Hirano Satoshi|Yamazaki Yoichi|Kamikubo Hironari|Kataoka Mikio | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1STN_A:W140Y","type":"_PDB_CH... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6698,"numValue":38.6,"references":[],"strValue":... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,710 | train | mutant | 861 | 117 | 968 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222Y | W222Y | 1 | 1 | 0 | 0 | 222 | W | Y | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 12,975 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | 20 | NaCl | 50 mM | 1STN_A:W140Y | null | null | 5 | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BU... | [{"datasets":[],"id":47377,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":47378,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47379,"numValue":null,"references":[],"strValue":"yes","type... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,712 | train | mutant | 862 | 117 | 969 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222L | W222L | 1 | 1 | 0 | 0 | 222 | W | L | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 12,976 | ProTherm | 7 | CD | Thermal | sodium phosphate | 25mM | 20 | NaCl | 50 mM | 1STN_A:W140L | null | null | 1.6 | 4.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 159 | ARTICLE | Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. | 2,004 | 10.1016/j.jmb.2004.02.044 | 15066439 | J Mol Biol;338;383-400 | 5 | Maki Kosuke|Cheng Hong|Dolgikh Dimitry A|Shastry M C Ramachandra|Roder Heinrich | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25mM","type":"BU... | [{"datasets":[],"id":47380,"numValue":1.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":47381,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47382,"numValue":null,"references":[],"strValue":"yes","type... | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,713 | train | mutant | 4,440 | 117 | 4,958 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222A | W222A | 1 | 1 | 0 | 0 | 222 | W | A | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 10,523 | ProTherm | 5 | Fluorescence | GdnHCl | Phosphate | 25 | 1STN_A:W140A | null | null | null | null | null | null | null | 0.15 | 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:W140A",... | [{"datasets":[],"id":36162,"numValue":0.15,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":36163,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,715 | train | mutant | 4,440 | 117 | 4,958 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | W222A | W222A | 1 | 1 | 0 | 0 | 222 | W | A | 9 | CONSERVATION | 1STN | 140 | null | 222 | A | G | true | false | 57.674272 | 22.261429 | 10,525 | ProTherm | 8.8 | Fluorescence | Activity | Tris-HCl | 25 mM | 25 | Calcium chloride | 10 mM | 1STN_A:W140A | null | null | null | null | null | null | null | 0.15 | 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":36166,"numValue":0.15,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":36167,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7992,"numValue":9.0,"position":222,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,718 | train | mutant | 901 | 117 | 1,018 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S223A | S223A | 1 | 1 | 0 | 0 | 223 | S | A | 9 | CONSERVATION | 1STN | 140 | null | 223 | A | L | false | false | 105.678188 | 31.606666 | 2,501 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1STN_A:S141A | 52.6 | -0.4 | null | null | null | null | 82 | 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":9214,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9215,"numValue":-0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9216,"numValue":82.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9217,"numValue":null,"references":[],"... | [{"id":7993,"numValue":9.0,"position":223,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:7719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,719 | train | mutant | 901 | 117 | 1,018 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S223A | S223A | 1 | 1 | 0 | 0 | 223 | S | A | 9 | CONSERVATION | 1STN | 140 | null | 223 | A | L | false | false | 105.678188 | 31.606666 | 8,097 | ProTherm | 7 | CD | Thermal | MOPS | 10 mM | 40 | 1STN_A:S141A | null | null | 2.13 | 0.12 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 170 | ARTICLE | Role of C-terminal region of Staphylococcal nuclease for foldability, stability, and activity. | 2,002 | 10.1002/prot.10216 | 12211005 | Proteins;49;255-65 | 6 | Hirano Satoshi|Mihara Ken'ichi|Yamazaki Yoichi|Kamikubo Hironari|Imamoto Yasushi|Kataoka Mikio | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":27530,"numValue":2.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":27531,"numValue":0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27532,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7993,"numValue":9.0,"position":223,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,720 | train | mutant | 901 | 117 | 1,018 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S223A | S223A | 1 | 1 | 0 | 0 | 223 | S | A | 9 | CONSERVATION | 1STN | 140 | null | 223 | A | L | false | false | 105.678188 | 31.606666 | 13,080 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:S141A | null | null | 5.1 | 0.4 | null | null | null | 0.75 | 1 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|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":47869,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":47870,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47871,"numValue":1.0,"references"... | [{"id":7993,"numValue":9.0,"position":223,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,721 | train | mutant | 6,164 | 117 | 6,752 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S223G | S223G | 1 | 1 | 0 | 0 | 223 | S | G | 9 | CONSERVATION | 1STN | 140 | null | 223 | A | L | false | false | 105.678188 | 31.606666 | 13,079 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1STN_A:S141G | null | null | 4.6 | 0.9 | null | null | null | 0.69 | 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 | 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":47864,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":47865,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47866,"numValue":0.98,"references":[],"strValue":nu... | [{"id":7993,"numValue":9.0,"position":223,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:7722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,722 | train | mutant | 5,977 | 117 | 6,547 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E224A | E224A | 1 | 1 | 0 | 0 | 224 | E | A | 5 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,850 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:E142A | null | null | 5.3 | 0.3 | null | null | null | 0.76 | 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 | 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":46766,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46767,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46768,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46769,"numValue":0.76,"references":[],"s... | [{"id":7994,"numValue":5.0,"position":224,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,723 | train | mutant | 5,978 | 117 | 6,548 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | E224G | E224G | 1 | 1 | 0 | 0 | 224 | E | G | 5 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,851 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:E142G | null | null | 5.3 | 0.3 | null | null | null | 0.76 | 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 | 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":46771,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46772,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46773,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46774,"numValue":0.76,"references":[],"s... | [{"id":7994,"numValue":5.0,"position":224,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,724 | train | mutant | 1,299 | 117 | 1,449 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D225F | D225F | 1 | 1 | 0 | 0 | 225 | D | F | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 2,463 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1JOK_A:D143F | 51.2 | -1.5 | null | null | null | null | 91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"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":9062,"numValue":51.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9063,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv"],"id":9064,"numValue":91.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9065,"numValue":null,"... | [{"id":7995,"numValue":7.0,"position":225,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,726 | train | mutant | 1,299 | 117 | 1,449 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D225F | D225F | 1 | 1 | 0 | 0 | 225 | D | F | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 13,379 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 600 mM | 1JOK_A:D143F | null | null | 5.4 | 0.1 | null | null | null | 0.83 | 0.98 | 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 | 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":49250,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":49251,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":49252,"numValue":0.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":49253,"numValue":0.83,"references":[],"s... | [{"id":7995,"numValue":7.0,"position":225,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,727 | train | mutant | 5,954 | 117 | 6,524 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D225A | D225A | 1 | 1 | 0 | 0 | 225 | D | A | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,824 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:D143A | null | null | 5.5 | 0.1 | null | null | null | 0.79 | 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 | 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":46636,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46637,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46638,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46639,"numValue":0.79,"references":[],"s... | [{"id":7995,"numValue":7.0,"position":225,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,728 | train | mutant | 5,955 | 117 | 6,525 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D225G | D225G | 1 | 1 | 0 | 0 | 225 | D | G | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,825 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:D143G | null | null | 5.4 | 0.2 | null | null | null | 0.79 | 0.98 | 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 | 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":46641,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46642,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46643,"numValue":0.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46644,"numValue":0.79,"references":[],"s... | [{"id":7995,"numValue":7.0,"position":225,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,729 | train | mutant | 6,079 | 117 | 6,664 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D225K | D225K | 1 | 1 | 0 | 0 | 225 | D | K | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,956 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1JOK_A:D143K | null | null | 5.1 | 0.3 | null | null | null | 0.78 | 6.47 | 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 | 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":47296,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":47297,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47298,"numValue":6.47,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47299,"numValue":0.78,"references":[],"s... | [{"id":7995,"numValue":7.0,"position":225,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,730 | train | mutant | 6,080 | 117 | 6,665 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D225N | D225N | 1 | 1 | 0 | 0 | 225 | D | N | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,957 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 25 mM | 20 | sodium chloride | 100 mM | 1JOK_A:D143N | null | null | 5.1 | 0.3 | null | null | null | 0.8 | 6.34 | 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 | 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":47301,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":47302,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47303,"numValue":6.34,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47304,"numValue":0.8,"references":[],"st... | [{"id":7995,"numValue":7.0,"position":225,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,731 | train | mutant | 6,111 | 117 | 6,699 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | A227G | A227G | 1 | 1 | 0 | 0 | 227 | A | G | 6 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 13,022 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:A145G | null | null | 5.1 | 0.4 | null | null | null | 0.8 | 0.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":47581,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":47582,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47583,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47584,"numValue":0.8,"references":[],"st... | [{"id":7997,"numValue":6.0,"position":227,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,733 | train | mutant | 5,956 | 117 | 6,526 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D228A | D228A | 1 | 1 | 0 | 0 | 228 | D | A | 6 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,826 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:D146A | null | null | 5.4 | 0.2 | null | null | null | 0.78 | 0.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46646,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46647,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46648,"numValue":0.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46649,"numValue":0.78,"references":[],"s... | [{"id":7998,"numValue":6.0,"position":228,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,734 | train | mutant | 5,957 | 117 | 6,527 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | D228G | D228G | 1 | 1 | 0 | 0 | 228 | D | G | 6 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 12,827 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:D146G | null | null | 5.4 | 0.2 | null | null | null | 0.78 | 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 | 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":46651,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":46652,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":46653,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":46654,"numValue":0.78,"references":[],"s... | [{"id":7998,"numValue":6.0,"position":228,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,735 | train | mutant | 1,243 | 117 | 1,393 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S229A | S229A | 1 | 1 | 0 | 0 | 229 | S | A | 8 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 2,407 | ProTherm | 7 | CD | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1JOK_A:S147A | 52.1 | -0.6 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 225 | ARTICLE | Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. | 2,007 | 10.1016/j.bpc.2006.10.014 | 17134819 | Biophys Chem;125;490-6 | 2 | Byrne Michael P|Stites Wesley E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"nu... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8838,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8839,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":884... | [{"id":7999,"numValue":8.0,"position":229,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,736 | train | mutant | 1,243 | 117 | 1,393 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | S229A | S229A | 1 | 1 | 0 | 0 | 229 | S | A | 8 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 2,502 | ProTherm | 7 | Fluorescence | Thermal | Phosphate | 25 mM | null | NaCl | 100 mM | 1JOK_A:S147A | 53.5 | 0.5 | null | null | null | null | 87 | 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":9218,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9219,"numValue":0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9220,"numValue":87.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":9221,"numValue":null,"references":[],"s... | [{"id":7999,"numValue":8.0,"position":229,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,737 | train | mutant | 6,161 | 117 | 6,749 | 231 | 231 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | Q231G | Q231G | 1 | 1 | 0 | 0 | 231 | Q | G | 7 | CONSERVATION | 1STN | 140 | null | false | false | null | null | 13,074 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | 1JOK_A:Q149G | null | null | 5.1 | 0.4 | null | null | null | 0.78 | 0.95 | 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 | 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":47839,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":47840,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":47841,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":47842,"numValue":0.78,"references":[],"s... | [{"id":8001,"numValue":7.0,"position":231,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7738 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,738 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,364 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 85.3 | null | null | null | null | 1.9 | null | null | null | null | null | null | null | null | null | null | yes | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 283 | ARTICLE | Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. | 1,995 | 10.1021/bi00007a007 | 7857925 | Biochemistry;34;2148-52 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Thomson J A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67765,"numValue":85.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67766,"numValue":1.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67767,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,739 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,538 | ProTherm | 7 | CD | Thermal | phosphate | 50 mM | null | 82 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1116 | ARTICLE | Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin. | 1,987 | 10.1021/bi00379a029 | 3552046 | Biochemistry;26;1406-11 | 4 | Shalongo W|Stellwagen E|Kelley R F|Jagannadham M V | [{"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":68388,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68389,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,740 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,707 | ProTherm | 7 | DSC | Thermal | phosphate | 0.01 M | null | NaCl | 0.1 M | 87 | null | null | null | 106.9 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1135 | ARTICLE | A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. | 1,992 | 10.1021/bi00135a022 | 1591250 | Biochemistry;31;4901-7 | 2 | Bolen D W|Santoro M M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":68972,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68973,"numValue":106.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":68974,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,741 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,774 | ProTherm | 6 | DSC | Thermal | Sodium phosphate | 50 mM | null | 74.01 | null | null | null | 67.78 | 1.93 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 910 | ARTICLE | Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. | 1,994 | 10.1021/bi00178a027 | 8142367 | Biochemistry;33;3688-92 | 5 | Wynn R|Kishore N|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69195,"numValue":74.01,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69196,"numValue":67.78,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69197,"numValue":1.93,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69198,"numValue":null,"references":... | ||||||||||||||||||||||||||
fireprotdb:7742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,742 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,775 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 73.34 | null | null | null | 76.11 | 2.07 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 910 | ARTICLE | Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. | 1,994 | 10.1021/bi00178a027 | 8142367 | Biochemistry;33;3688-92 | 5 | Wynn R|Kishore N|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69199,"numValue":73.34,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69200,"numValue":76.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69201,"numValue":2.07,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69202,"numValue":null,"references":... | ||||||||||||||||||||||||||
fireprotdb:7743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,743 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,795 | ProTherm | 6 | DSC | Thermal | Sodium phosphate | 50 mM | null | 88.44 | null | null | null | 83.4 | 0.98 | 101.7 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69283,"numValue":88.44,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69284,"numValue":83.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69285,"numValue":0.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69286,"numValue":101.7,"references":... | ||||||||||||||||||||||||||
fireprotdb:7744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,744 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,796 | ProTherm | 6.5 | DSC | Thermal | Sodium phosphate | 50 mM | null | 86.43 | null | null | null | 106.12 | 1.76 | 106.12 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69288,"numValue":86.43,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69289,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69290,"numValue":1.76,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69291,"numValue":106.12,"reference... | ||||||||||||||||||||||||||
fireprotdb:7746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,746 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,798 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 86.01 | null | null | null | 96.53 | 1.3 | 110 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69298,"numValue":86.01,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69299,"numValue":96.53,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69300,"numValue":1.3,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69301,"numValue":110.0,"references":... | ||||||||||||||||||||||||||
fireprotdb:7747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,747 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,799 | ProTherm | 7.25 | DSC | Thermal | Sodium phosphate | 50 mM | null | 85.05 | null | null | null | 96.76 | 0.95 | 118 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":7.25,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69303,"numValue":85.05,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69304,"numValue":96.76,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69305,"numValue":0.95,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69306,"numValue":118.0,"references"... | ||||||||||||||||||||||||||
fireprotdb:7748 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,748 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,800 | ProTherm | 7.5 | DSC | Thermal | Sodium phosphate | 50 mM | null | 83.48 | null | null | null | 97.34 | 1.9 | 120.7 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69308,"numValue":83.48,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69309,"numValue":97.34,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69310,"numValue":1.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69311,"numValue":120.7,"references":... | ||||||||||||||||||||||||||
fireprotdb:7749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,749 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,801 | ProTherm | 7.75 | DSC | Thermal | Sodium phosphate | 50 mM | null | 83.9 | null | null | null | 91.26 | 2.28 | 119.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":7.75,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69313,"numValue":83.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69314,"numValue":91.26,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69315,"numValue":2.28,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69316,"numValue":119.6,"references":... | ||||||||||||||||||||||||||
fireprotdb:7750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,750 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,802 | ProTherm | 8 | DSC | Thermal | Sodium phosphate | 50 mM | null | 83.3 | null | null | null | 85.88 | 3.84 | 119.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1157 | ARTICLE | Stability of oxidized Escherichia coli thioredoxin and its dependence on protonation of the aspartic acid residue in the 26 position. | 1,993 | 10.1021/bi00080a026 | 8393344 | Biochemistry;32;7526-30 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69318,"numValue":83.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69319,"numValue":85.88,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":69320,"numValue":3.84,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":69321,"numValue":119.4,"references":... | ||||||||||||||||||||||||||
fireprotdb:7751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,751 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,502 | ProTherm | 7 | DSC | Thermal | phosphate | 0.01 M | 25 | NaCl | 0.1 M | null | null | 8.9 | null | null | 1.66 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1135 | ARTICLE | A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. | 1,992 | 10.1021/bi00135a022 | 1591250 | Biochemistry;31;4901-7 | 2 | Bolen D W|Santoro M M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER... | [{"datasets":[],"id":74930,"numValue":1.66,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":74931,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74932,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,752 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,749 | ProTherm | 8.7 | CD | Urea | Tris | 0.375 M | 25 | null | null | 10 | null | null | null | null | 7.4 | null | null | null | null | null | null | null | null | Unknown | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1381 | ARTICLE | Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation. | 1,989 | 10.1021/bi00434a015 | 2663067 | Biochemistry;28;3211-20 | 3 | Langsetmo K|Woodward C|Fuchs J | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.375 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75775,"numValue":10.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75776,"numValue":7.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75777,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,753 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,750 | ProTherm | 8.7 | CD | Urea | Tris | 0.375 M | 25 | null | null | 6.5 | null | null | null | null | 4.4 | null | null | null | null | null | null | null | null | Unknown | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1381 | ARTICLE | Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation. | 1,989 | 10.1021/bi00434a015 | 2663067 | Biochemistry;28;3211-20 | 3 | Langsetmo K|Woodward C|Fuchs J | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.375 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75778,"numValue":6.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75779,"numValue":4.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75780,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,754 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,762 | ProTherm | 7 | CD | GdnHCl | phosphate | 50 mM | 25 | null | null | 8.6 | null | null | null | null | 2.6 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1116 | ARTICLE | Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin. | 1,987 | 10.1021/bi00379a029 | 3552046 | Biochemistry;26;1406-11 | 4 | Shalongo W|Stellwagen E|Kelley R F|Jagannadham M V | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":75810,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75811,"numValue":2.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75812,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,755 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,763 | ProTherm | 7 | CD | Urea | phosphate | 50 mM | 25 | null | null | 8.7 | null | null | null | null | 6.7 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1116 | ARTICLE | Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin. | 1,987 | 10.1021/bi00379a029 | 3552046 | Biochemistry;26;1406-11 | 4 | Shalongo W|Stellwagen E|Kelley R F|Jagannadham M V | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":75813,"numValue":8.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75814,"numValue":6.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75815,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,757 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,776 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 50 mM | 25 | null | null | 8.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 703 | ARTICLE | Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. | 1,987 | 10.1021/bi00395a028 | 3322388 | Biochemistry;26;6765-74 | 2 | Kelley R F|Richards F M | [{"numValue":7.0,"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":75850,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75851,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,759 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,788 | ProTherm | 8.5 | CD | GdnHCl | Tris | 50 mM | 25 | null | null | 8.6 | null | null | null | null | null | 2.1 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":8.5,"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":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75889,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75890,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75891,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,760 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,789 | ProTherm | 8 | CD | GdnHCl | Tris | 50 mM | 25 | null | null | 8.8 | null | null | null | null | null | 2.2 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":8.0,"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":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75892,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75893,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75894,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,761 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,790 | ProTherm | 7.5 | CD | GdnHCl | TES | 50 mM | 25 | null | null | 9 | null | null | null | null | null | 2.2 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":7.5,"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":"TES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75895,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75896,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75897,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7762 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,762 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,791 | ProTherm | 7 | CD | GdnHCl | TES | 50 mM | 25 | null | null | 9.5 | null | null | null | null | null | 2.3 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":7.0,"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":"TES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75898,"numValue":9.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75899,"numValue":2.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75900,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,763 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,792 | ProTherm | 6.5 | CD | GdnHCl | ACES | 50 mM | 25 | null | null | 10 | null | null | null | null | null | 2.4 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":6.5,"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":"ACES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":75901,"numValue":10.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75902,"numValue":2.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75903,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,765 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,797 | ProTherm | 7 | DSC | GdnHCl | MOPS | 0.05 M | 25 | null | null | 7.8 | null | null | null | null | 2.22 | 3.51 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1135 | ARTICLE | A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. | 1,992 | 10.1021/bi00135a022 | 1591250 | Biochemistry;31;4901-7 | 2 | Bolen D W|Santoro M M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"... | [{"datasets":[],"id":75917,"numValue":7.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75918,"numValue":3.51,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75919,"numValue":2.22,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75920,"numValue":null,"references":[],"s... | ||||||||||||||||||||||||||
fireprotdb:7766 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,766 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,798 | ProTherm | 7 | DSC | Urea | MOPS | 0.05 M | 25 | NaCl | 0.5 M | null | null | 8.6 | null | null | null | null | 6.57 | 1.32 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1135 | ARTICLE | A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. | 1,992 | 10.1021/bi00135a022 | 1591250 | Biochemistry;31;4901-7 | 2 | Bolen D W|Santoro M M | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},... | [{"datasets":[],"id":75921,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75922,"numValue":1.32,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75923,"numValue":6.57,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75924,"numValue":null,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:7767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,767 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,466 | ProTherm | 8.7 | Absorbance | Urea | Tris | 0.1 M | 23 | KCl | 0.2 M | null | null | 6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 796 | ARTICLE | Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. | 1,991 | 10.1073/pnas.88.23.10573 | 1961723 | Proc Natl Acad Sci U S A;88;10573-7 | 2 | Kim P S|Lin T Y | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_C... | [{"datasets":[],"id":78006,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78007,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,768 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,467 | ProTherm | 8.7 | Absorbance | Urea | Tris | 0.1 M | 23 | KCl | 0.2 M | null | null | 9.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 796 | ARTICLE | Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. | 1,991 | 10.1073/pnas.88.23.10573 | 1961723 | Proc Natl Acad Sci U S A;88;10573-7 | 2 | Kim P S|Lin T Y | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_C... | [{"datasets":[],"id":78008,"numValue":9.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78009,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,769 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,487 | ProTherm | 8.7 | CD | GdnHCl | Tris-HCl | 0.1 M | 23 | KCl | 0.2 M | null | null | 5 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1486 | ARTICLE | Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. | 1,989 | 10.1021/bi00438a054 | 2669972 | Biochemistry;28;5282-7 | 2 | Kim P S|Lin T Y | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CON... | [{"datasets":[],"id":78072,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78073,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,770 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,488 | ProTherm | 8.7 | CD | GdnHCl | Tris-HCl | 0.1 M | 23 | KCl | 0.2 M | null | null | 8.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1486 | ARTICLE | Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. | 1,989 | 10.1021/bi00438a054 | 2669972 | Biochemistry;28;5282-7 | 2 | Kim P S|Lin T Y | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CON... | [{"datasets":[],"id":78074,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78075,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7771 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,771 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,735 | ProTherm | 5.7 | CD | GdnHCl | Potassium phosphate | 10 mM | 20 | null | null | 9.5 | null | null | null | null | 2.61 | 3.7 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1530 | ARTICLE | Energetics of assembling an artificial heterodimer with an alpha/beta motif: cleaved versus uncleaved Escherichia coli thioredoxin. | 1,999 | 10.1021/bi990498l | 10529211 | Biochemistry;38;13355-66 | 4 | Zhu D|Georgescu R E|Braswell E H|Tasayco M L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":78858,"numValue":9.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78859,"numValue":3.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78860,"numValue":2.61,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78861,"numValue":null,"references":[],"st... | ||||||||||||||||||||||||||
fireprotdb:7772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,772 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,318 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 87 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80603,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80604,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,773 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,013 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 89.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":82660,"numValue":89.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":82661,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,774 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,014 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 75.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":82662,"numValue":75.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":82663,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,775 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,390 | ProTherm | 7 | DSC | Thermal | Hepes | 5 mM | null | 89.05 | null | null | null | 102.77 | 1.39 | null | null | null | null | null | null | null | null | null | null | no | 2.0 | TM|DH|DCP|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":86604,"numValue":89.05,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86605,"numValue":102.77,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":86606,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":86607,"numValue":2.0,"references":... | |||||||||||||||||||||||||
fireprotdb:7776 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,776 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,023 | ProTherm | 7.4 | DSC | Thermal | CGH-10 | null | 87.3 | null | null | null | 112 | null | null | null | null | null | null | null | null | null | null | null | no | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 1777 | ARTICLE | Effect of signal peptide on stability and folding of Escherichia coli thioredoxin. | 2,013 | 10.1371/journal.pone.0063442 | 23667620 | PLoS One;8;e63442 | 8 | Varadarajan Raghavan|Prajapati Ravindra Singh|Ali P Shaik Syed|Singh Pranveer|Sharma Likhesh|Kulothungan S Rajendra|Adkar Bharat V|Krishnan Beena | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"CGH-10","type":"BUFFER"}] | [{"datasets":[],"id":88295,"numValue":87.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88296,"numValue":112.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":88297,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||||
fireprotdb:7777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,777 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,672 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | null | null | 7.9 | null | null | null | null | 2.5 | 3.2 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1811 | ARTICLE | Probing the structure and stability of a hybrid protein: the human-E. coli thioredoxin chimera. | 2,001 | 10.1021/bi010745x | 11551217 | Biochemistry;40;11184-92 | 5 | Tcherkasskaya O|Gronenborn A M|Georgescu R E|Tasayco M L|Louis J M | [{"numValue":7.0,"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":90099,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":90100,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":90101,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":90102,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:7778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,778 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,673 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 50 mM | 25 | null | null | 9 | null | null | null | null | 2.6 | 3.4 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":90103,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":90104,"numValue":3.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":90105,"numValue":2.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":90106,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:7779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,779 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,952 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 30 mM | 25 | KCl | 0.1 M | null | null | 9.6 | null | null | null | null | 2.5 | null | null | null | null | null | null | null | null | Unknown | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1828 | ARTICLE | Folding subdomains of thioredoxin characterized by native-state hydrogen exchange. | 2,003 | 10.1110/ps.0239503 | 12876321 | Protein Sci;12;1719-31 | 2 | Udgaonkar Jayant B|Bhutani Nidhi | [{"numValue":7.0,"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BU... | [{"datasets":[],"id":91221,"numValue":9.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91222,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":91223,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,780 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,953 | ProTherm | 7 | Fluorescence | GdnHCl | sodium phosphate | 30 mM | 25 | KCl | 0.1 M | null | null | 9.6 | null | null | null | null | 2.5 | null | null | null | null | null | null | null | null | Unknown | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1828 | ARTICLE | Folding subdomains of thioredoxin characterized by native-state hydrogen exchange. | 2,003 | 10.1110/ps.0239503 | 12876321 | Protein Sci;12;1719-31 | 2 | Udgaonkar Jayant B|Bhutani Nidhi | [{"numValue":7.0,"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM",... | [{"datasets":[],"id":91224,"numValue":9.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91225,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":91226,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7781 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,781 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,039 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | null | null | 9.6 | null | null | null | null | 2.6 | 3.7 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"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":"10 mM","type":... | [{"datasets":[],"id":91488,"numValue":9.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91489,"numValue":3.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":91490,"numValue":2.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":91491,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:7782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,782 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,040 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | null | null | 6.2 | null | null | null | null | 1.7 | 3.6 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"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":"10 mM","type":... | [{"datasets":[],"id":91492,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91493,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":91494,"numValue":1.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":91495,"numValue":null,"references":[],"str... | ||||||||||||||||||||||||||
fireprotdb:7783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,783 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,629 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | null | null | null | null | null | null | null | 6.92 | 1.28 | null | null | null | null | null | null | null | no | 2.0 | M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":93413,"numValue":1.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":93414,"numValue":6.92,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":93415,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":93416,"numValue":null,"references":[]... | |||||||||||||||||||||||||
fireprotdb:7784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,784 | train | sequence | 126 | 126 | -1 | 109 | -1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,783 | ProTherm | 7.4 | DSC | GdnHCl | CGH-10 | 25 | null | null | 8.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | no | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER | 1777 | ARTICLE | Effect of signal peptide on stability and folding of Escherichia coli thioredoxin. | 2,013 | 10.1371/journal.pone.0063442 | 23667620 | PLoS One;8;e63442 | 8 | Varadarajan Raghavan|Prajapati Ravindra Singh|Ali P Shaik Syed|Singh Pranveer|Sharma Likhesh|Kulothungan S Rajendra|Adkar Bharat V|Krishnan Beena | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"CGH-10","type":"BUFFER"}] | [{"datasets":[],"id":94020,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":94021,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||||
fireprotdb:7787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,787 | train | mutant | 4,958 | 126 | 5,509 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I6V | I6V | 1 | 1 | 0 | 0 | 6 | I | V | 3 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 6 | A | E | true | false | 60.995521 | 27.873125 | 11,542 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I5V | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39857,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39858,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39859,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8007,"numValue":3.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,788 | train | mutant | 4,947 | 126 | 5,498 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D11E | D11E | 1 | 1 | 0 | 0 | 11 | D | E | 2 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 11 | A | T | false | false | 138.357282 | 30.205625 | 11,529 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:D10E | null | null | null | 5.7 | null | null | null | 5.83 | 1.22 | null | null | null | null | null | null | null | no | 2.0 | DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39814,"numValue":5.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39815,"numValue":1.22,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":39816,"numValue":5.83,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":39817,"numValue":2.0,"references":[],"s... | [{"id":8012,"numValue":2.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,789 | train | mutant | 4,947 | 126 | 5,498 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D11E | D11E | 1 | 1 | 0 | 0 | 11 | D | E | 2 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 11 | A | T | false | false | 138.357282 | 30.205625 | 11,530 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:D10E | null | null | null | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39819,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39820,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39821,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8012,"numValue":2.0,"position":11,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,791 | train | mutant | 4,966 | 126 | 5,517 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | V17I | V17I | 1 | 1 | 0 | 0 | 17 | V | I | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 17 | A | T | false | false | 1.003129 | 22.892143 | 11,550 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:V16I | null | null | null | 3.4 | null | null | null | 6.27 | 1.24 | null | null | null | null | null | null | null | no | 2.0 | DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39883,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39884,"numValue":1.24,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":39885,"numValue":6.27,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":39886,"numValue":2.0,"references":[],"s... | [{"id":8018,"numValue":7.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,792 | train | mutant | 4,959 | 126 | 5,510 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I24V | I24V | 1 | 1 | 0 | 0 | 24 | I | V | 8 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 24 | A | E | false | false | 5.03891 | 22.786875 | 11,543 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I23V | null | null | null | -1.1 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39860,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39861,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39862,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8025,"numValue":8.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,793 | train | mutant | 4,967 | 126 | 5,518 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | V26I | V26I | 1 | 1 | 0 | 0 | 26 | V | I | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 26 | A | E | false | false | 0 | 18.617857 | 11,551 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:V25I | null | null | null | 3.8 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39888,"numValue":3.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39889,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39890,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8027,"numValue":9.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,794 | train | mutant | 256 | 126 | 287 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D27I | D27I | 1 | 1 | 0 | 0 | 27 | D | I | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 27 | A | E | true | true | 1.871887 | 21.565 | 462 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 2TRX_A:D26I | 98 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:D26I","typ... | [{"datasets":[],"id":1856,"numValue":98.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1857,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8028,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,795 | train | mutant | 256 | 126 | 287 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D27I | D27I | 1 | 1 | 0 | 0 | 27 | D | I | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 27 | A | E | true | true | 1.871887 | 21.565 | 8,757 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 50 mM | 25 | 2TRX_A:D26I | null | null | null | -12.1 | null | null | null | 3.7 | 3.3 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":29579,"numValue":-12.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29580,"numValue":3.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29581,"numValue":3.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29582,"numValue":null,"references":[],"... | [{"id":8028,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,796 | train | mutant | 4,566 | 126 | 5,086 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D27A | D27A | 1 | 1 | 0 | 0 | 27 | D | A | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 27 | A | E | true | true | 1.871887 | 21.565 | 10,745 | ProTherm | 8.5 | CD | GdnHCl | Tris | 50 mM | 25 | 2TRX_A:D26A | null | null | 13.2 | -4.6 | null | null | null | null | 3.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":8.5,"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":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":36949,"numValue":13.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36950,"numValue":-4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36951,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36952,"numValue":null,"references":[],"... | [{"id":8028,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7797 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,797 | train | mutant | 4,566 | 126 | 5,086 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D27A | D27A | 1 | 1 | 0 | 0 | 27 | D | A | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 27 | A | E | true | true | 1.871887 | 21.565 | 10,746 | ProTherm | 8 | CD | GdnHCl | Tris | 50 mM | 25 | 2TRX_A:D26A | null | null | 13.2 | -4.4 | null | null | null | null | 3.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":8.0,"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":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":36953,"numValue":13.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36954,"numValue":-4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36955,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36956,"numValue":null,"references":[],"... | [{"id":8028,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,798 | train | mutant | 4,566 | 126 | 5,086 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D27A | D27A | 1 | 1 | 0 | 0 | 27 | D | A | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 27 | A | E | true | true | 1.871887 | 21.565 | 10,747 | ProTherm | 7.5 | CD | GdnHCl | TES | 50 mM | 25 | 2TRX_A:D26A | null | null | 13.2 | -4.2 | null | null | null | null | 3.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":7.5,"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":"TES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":36957,"numValue":13.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":36958,"numValue":-4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36959,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36960,"numValue":null... | [{"id":8028,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,799 | train | mutant | 4,566 | 126 | 5,086 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D27A | D27A | 1 | 1 | 0 | 0 | 27 | D | A | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 27 | A | E | true | true | 1.871887 | 21.565 | 10,748 | ProTherm | 7 | CD | GdnHCl | TES | 50 mM | 25 | 2TRX_A:D26A | null | null | 13.2 | -3.7 | null | null | null | null | 3.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 704 | ARTICLE | The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability. | 1,991 | 10.1021/bi00244a032 | 1854757 | Biochemistry;30;7603-9 | 3 | Langsetmo K|Woodward C|Fuchs J A | [{"numValue":7.0,"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":"TES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":36961,"numValue":13.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36962,"numValue":-3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36963,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36964,"numValue":null,"references":[],"... | [{"id":8028,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7800 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,800 | train | mutant | 4,953 | 126 | 5,504 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | E31D | E31D | 1 | 1 | 0 | 0 | 31 | E | D | 3 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 31 | A | T | true | false | 109.725256 | 34.717778 | 11,536 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:E30D | null | null | null | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39837,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39838,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39839,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8032,"numValue":3.0,"position":31,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,801 | train | mutant | 257 | 126 | 288 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33A | C33A | 1 | 1 | 0 | 0 | 33 | C | A | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33 | A | L | true | false | 6.147471 | 29.6175 | 463 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 2TRX_A:C32A | 74 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32A","typ... | [{"datasets":[],"id":1858,"numValue":74.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1859,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,802 | train | mutant | 257 | 126 | 288 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33A | C33A | 1 | 1 | 0 | 0 | 33 | C | A | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33 | A | L | true | false | 6.147471 | 29.6175 | 8,758 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 50 mM | 25 | 2TRX_A:C32A | null | null | null | -5.3 | null | null | null | 1.6 | 3.4 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":["SAAFEC_S1262.csv"],"id":29583,"numValue":-5.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29584,"numValue":3.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29585,"numValue":1.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29586,"numValue":null,... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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