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:6227 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,227 | train | mutant | 463 | 76 | 512 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | R88M | R88M | 1 | 1 | 0 | 0 | 88 | R | M | 4 | CONSERVATION | 1BPI | 57 | null | 88 | A | H | false | false | 171.736502 | 8.863636 | 756 | ProTherm | 4.3 | DSC | Thermal | acetate/Na | 10 mM | null | 1BPI_A:R53M | 97.3 | null | null | null | 75.1 | null | 77.8 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 84 | ARTICLE | Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI). | 2,002 | 10.1110/ps.4460102 | 11910035 | Protein Sci;11;924-32 | 3 | Buczek Olga|Krowarsch Daniel|Otlewski Jacek | [{"numValue":4.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate/Na","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BPI_A:R53M","type":"_... | [{"datasets":[],"id":2891,"numValue":97.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2892,"numValue":75.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2893,"numValue":77.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":2894,"numValue":null,"references":[],"s... | [{"id":7674,"numValue":4.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:6228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,228 | train | mutant | 463 | 76 | 512 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | R88M | R88M | 1 | 1 | 0 | 0 | 88 | R | M | 4 | CONSERVATION | 1BPI | 57 | null | 88 | A | H | false | false | 171.736502 | 8.863636 | 8,858 | ProTherm | 4.3 | DSC | Thermal | GlyGly/HCl | 10 mM | 25 | 1BPI_A:R53M | null | null | 12.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 84 | ARTICLE | Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI). | 2,002 | 10.1110/ps.4460102 | 11910035 | Protein Sci;11;924-32 | 3 | Buczek Olga|Krowarsch Daniel|Otlewski Jacek | [{"numValue":4.3,"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":"GlyGly/HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":30003,"numValue":12.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30004,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7674,"numValue":4.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:6229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,229 | train | mutant | 1,588 | 76 | 1,787 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | R88A | R88A | 1 | 1 | 0 | 0 | 88 | R | A | 4 | CONSERVATION | 1BPI | 57 | null | 88 | A | H | false | false | 171.736502 | 8.863636 | 2,980 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | null | NaCl | 150 mM | 1BPI_A:R53A | 38.3 | -0.9 | null | null | 45 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S1634.cs... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10815,"numValue":38.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3... | [{"id":7674,"numValue":4.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6230 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,230 | train | mutant | 1,588 | 76 | 1,787 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | R88A | R88A | 1 | 1 | 0 | 0 | 88 | R | A | 4 | CONSERVATION | 1BPI | 57 | null | 88 | A | H | false | false | 171.736502 | 8.863636 | 8,199 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | 39 | NaCl | 150 mM | 1BPI_A:R53A | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":39.0,"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":"10 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27788,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27789,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7674,"numValue":4.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,231 | train | mutant | 464 | 76 | 513 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | T89M | T89M | 1 | 1 | 0 | 0 | 89 | T | M | 5 | CONSERVATION | 1BPI | 57 | null | 89 | A | H | false | false | 50.133747 | 8.158571 | 757 | ProTherm | 4.3 | DSC | Thermal | acetate/Na | 10 mM | null | 1BPI_A:T54M | 98.6 | null | null | null | 78.2 | null | 76.8 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 84 | ARTICLE | Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI). | 2,002 | 10.1110/ps.4460102 | 11910035 | Protein Sci;11;924-32 | 3 | Buczek Olga|Krowarsch Daniel|Otlewski Jacek | [{"numValue":4.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate/Na","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BPI_A:T54M","type":"_... | [{"datasets":[],"id":2895,"numValue":98.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2896,"numValue":78.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2897,"numValue":76.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":2898,"numValue":null,"references":[],"s... | [{"id":7675,"numValue":5.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:6232 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,232 | train | mutant | 464 | 76 | 513 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | T89M | T89M | 1 | 1 | 0 | 0 | 89 | T | M | 5 | CONSERVATION | 1BPI | 57 | null | 89 | A | H | false | false | 50.133747 | 8.158571 | 8,859 | ProTherm | 4.3 | DSC | Thermal | GlyGly/HCl | 10 mM | 25 | 1BPI_A:T54M | null | null | 12 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 84 | ARTICLE | Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI). | 2,002 | 10.1110/ps.4460102 | 11910035 | Protein Sci;11;924-32 | 3 | Buczek Olga|Krowarsch Daniel|Otlewski Jacek | [{"numValue":4.3,"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":"GlyGly/HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":30005,"numValue":12.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30006,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7675,"numValue":5.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:6233 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,233 | train | mutant | 1,589 | 76 | 1,788 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | T89A | T89A | 1 | 1 | 0 | 0 | 89 | T | A | 5 | CONSERVATION | 1BPI | 57 | null | 89 | A | H | false | false | 50.133747 | 8.158571 | 2,981 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | null | NaCl | 150 mM | 1BPI_A:T54A | 38.5 | -0.7 | null | null | 43 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":10819,"numValue":38.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10820,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10821,"numValue":43.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7675,"numValue":5.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6234 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,234 | train | mutant | 1,589 | 76 | 1,788 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | T89A | T89A | 1 | 1 | 0 | 0 | 89 | T | A | 5 | CONSERVATION | 1BPI | 57 | null | 89 | A | H | false | false | 50.133747 | 8.158571 | 8,200 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | 39 | NaCl | 150 mM | 1BPI_A:T54A | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":39.0,"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":"10 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27790,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27791,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7675,"numValue":5.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,235 | train | mutant | 1,590 | 76 | 1,789 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | G91A | G91A | 1 | 1 | 0 | 0 | 91 | G | A | 4 | CONSERVATION | 1BPI | 57 | null | 91 | A | S | false | false | 20.009653 | 8.3 | 2,982 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | null | NaCl | 150 mM | 1BPI_A:G56A | 37.8 | -1.4 | null | null | 43 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":10823,"numValue":37.8,"references":[],"strValue":null,"type":"TM"},{"data... | [{"id":7677,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6236 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,236 | train | mutant | 1,590 | 76 | 1,789 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | G91A | G91A | 1 | 1 | 0 | 0 | 91 | G | A | 4 | CONSERVATION | 1BPI | 57 | null | 91 | A | S | false | false | 20.009653 | 8.3 | 8,201 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | 39 | NaCl | 150 mM | 1BPI_A:G56A | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":39.0,"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":"10 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27792,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27793,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7677,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,238 | train | mutant | 1,591 | 76 | 1,790 | 100 | 100 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | 9 | Pancreatic trypsin inhibitor | Bos taurus | 1 | P00974 | IPR002223|IPR036880|IPR020901|IPR050098 | G92A | G92A | 1 | 1 | 0 | 0 | 92 | G | A | 5 | CONSERVATION | 1BPI | 57 | null | 92 | A | L | false | false | 40.671278 | 10.9025 | 8,202 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | 39 | NaCl | 150 mM | 1BPI_A:G57A | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 262 | ARTICLE | Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. | 1,995 | 10.1006/jmbi.1995.0304 | 7540212 | J Mol Biol;249;388-97 | 3 | Yu M H|Weissman J S|Kim P S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":39.0,"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":"10 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27794,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27795,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":7678,"numValue":5.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:6239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,239 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,510 | ProTherm | 4.15 | CD | Thermal | acetate | 10 mM | null | 74.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":4.15,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64586,"numValue":74.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64587,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6240 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,240 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,472 | ProTherm | 6.3 | DSC | GdnHCl | MES-NaOH | 50 mM | 25 | null | null | 7.16 | null | null | null | null | 4.05 | 1.76 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":6.3,"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":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":74837,"numValue":7.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74838,"numValue":1.76,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":74839,"numValue":4.05,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":74840,"numValue":null,"references":[],"... | ||||||||||||||||||||||||||||
fireprotdb:6241 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,241 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,533 | ProTherm | 2.2 | DSC | Thermal | glycine-HCl | 10 mM | 25 | null | null | 1.94 | null | null | 0.79 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1087 | ARTICLE | Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. | 1,991 | 10.1021/bi00107a010 | 1931967 | Biochemistry;30;10428-35 | 2 | Fersht A R|Jackson S E | [{"numValue":2.2,"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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFE... | [{"datasets":[],"id":75018,"numValue":0.79,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":75019,"numValue":1.94,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75020,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6242 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,242 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,534 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 10 mM | 25 | null | null | 2.79 | null | null | 0.79 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1087 | ARTICLE | Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. | 1,991 | 10.1021/bi00107a010 | 1931967 | Biochemistry;30;10428-35 | 2 | Fersht A R|Jackson S E | [{"numValue":2.5,"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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFE... | [{"datasets":[],"id":75021,"numValue":0.79,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":75022,"numValue":2.79,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75023,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,243 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,535 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 10 mM | 25 | null | null | 3.73 | null | null | 0.79 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1087 | ARTICLE | Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. | 1,991 | 10.1021/bi00107a010 | 1931967 | Biochemistry;30;10428-35 | 2 | Fersht A R|Jackson S E | [{"numValue":2.8,"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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFE... | [{"datasets":[],"id":75024,"numValue":0.79,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":75025,"numValue":3.73,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75026,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6244 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,244 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,536 | ProTherm | 3.2 | DSC | Thermal | glycine-HCl | 10 mM | 25 | null | null | 5.2 | null | null | 0.79 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1087 | ARTICLE | Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. | 1,991 | 10.1021/bi00107a010 | 1931967 | Biochemistry;30;10428-35 | 2 | Fersht A R|Jackson S E | [{"numValue":3.2,"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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFE... | [{"datasets":[],"id":75027,"numValue":0.79,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":75028,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75029,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6245 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,245 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,537 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 10 mM | 25 | null | null | 6.48 | null | null | 0.79 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1087 | ARTICLE | Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. | 1,991 | 10.1021/bi00107a010 | 1931967 | Biochemistry;30;10428-35 | 2 | Fersht A R|Jackson S E | [{"numValue":3.5,"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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFE... | [{"datasets":[],"id":75030,"numValue":0.79,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":75031,"numValue":6.48,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75032,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6246 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,246 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,328 | ProTherm | 6.3 | Fluorescence | GdnHCl | Sodium phosphate | 20 mM | 25 | null | null | 7.41 | null | null | null | null | null | 1.96 | null | null | null | null | null | null | null | unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1850 | ARTICLE | Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification. | 2,006 | 10.1110/ps.051851506 | 16452617 | Protein Sci;15;640-6 | 3 | J?ger Marcus|Nir Eyal|Weiss Shimon | [{"numValue":6.3,"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":"20 mM",... | [{"datasets":[],"id":92414,"numValue":7.41,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":92415,"numValue":1.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":92416,"numValue":null,"references":[],"strValue":"unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6247 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,247 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,329 | ProTherm | 6.3 | Fluorescence | GdnHCl | Sodium phosphate | 20 mM | 25 | null | null | 7.27 | null | null | null | null | null | 2.01 | null | null | null | null | null | null | null | unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1850 | ARTICLE | Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification. | 2,006 | 10.1110/ps.051851506 | 16452617 | Protein Sci;15;640-6 | 3 | J?ger Marcus|Nir Eyal|Weiss Shimon | [{"numValue":6.3,"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":"20 mM",... | [{"datasets":[],"id":92417,"numValue":7.27,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":92418,"numValue":2.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":92419,"numValue":null,"references":[],"strValue":"unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6248 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,248 | train | sequence | 95 | 95 | -1 | 84 | -1 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,330 | ProTherm | 6.3 | Fluorescence | GdnHCl | Sodium phosphate | 20 mM | 25 | null | null | 7.22 | null | null | null | null | null | 1.96 | null | null | null | null | null | null | null | unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1850 | ARTICLE | Site-specific labeling of proteins for single-molecule FRET by combining chemical and enzymatic modification. | 2,006 | 10.1110/ps.051851506 | 16452617 | Protein Sci;15;640-6 | 3 | J?ger Marcus|Nir Eyal|Weiss Shimon | [{"numValue":6.3,"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":"20 mM",... | [{"datasets":[],"id":92420,"numValue":7.22,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":92421,"numValue":1.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":92422,"numValue":null,"references":[],"strValue":"unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:6249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,249 | train | mutant | 86 | 95 | 96 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | K44A | K44A | 1 | 1 | 0 | 0 | 44 | K | A | 7 | CONSERVATION | null | false | false | null | null | 143 | ProTherm | 4.15 | CD | Thermal | acetate | 10 mM | null | 2CI2_I:K43A | 73 | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":4.15,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2CI2_I:K43A","type":"_PDB... | [{"datasets":[],"id":566,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv"],"id":567,"numValue":1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":568,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":7730,"numValue":7.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:6250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,250 | train | mutant | 86 | 95 | 96 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | K44A | K44A | 1 | 1 | 0 | 0 | 44 | K | A | 7 | CONSERVATION | null | false | false | null | null | 145 | ProTherm | 4.15 | CD | Thermal | acetate | 10 mM | null | 2CI2_I:K43A | 74.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":4.15,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2CI2_I:K43A","type":"_PDB... | [{"datasets":[],"id":572,"numValue":74.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv"],"id":573,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":7730,"numValue":7.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:6251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,251 | train | mutant | 86 | 95 | 96 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | K44A | K44A | 1 | 1 | 0 | 0 | 44 | K | A | 7 | CONSERVATION | null | false | false | null | null | 6,569 | ProTherm | 4.15 | CD | Thermal | acetate | 10 mM | 74.3 | 2CI2_I:K43A | null | null | null | -0.26 | null | null | null | null | null | null | null | null | null | null | null | null | no | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":4.15,"strValue":null,"type":"PH"},{"numValue":74.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CO... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":23489,"numValue":-0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23490,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":7730,"numValue":7.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:6252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,252 | train | mutant | 86 | 95 | 96 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | K44A | K44A | 1 | 1 | 0 | 0 | 44 | K | A | 7 | CONSERVATION | null | false | false | null | null | 8,602 | ProTherm | 6.3 | DSC | GdnHCl | MES-NaOH | 50 mM | 25 | 2CI2_I:K43A | null | null | 6.52 | null | null | null | null | 3.69 | 1.76 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":6.3,"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":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":29194,"numValue":6.52,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29195,"numValue":1.76,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29196,"numValue":3.69,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29197,"numValue":null,"references":[],"... | [{"id":7730,"numValue":7.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:6253 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,253 | train | mutant | 86 | 95 | 96 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | K44A | K44A | 1 | 1 | 0 | 0 | 44 | K | A | 7 | CONSERVATION | null | false | false | null | null | 8,604 | ProTherm | 6.3 | DSC | GdnHCl | MES-NaOH | 50 mM | 25 | 2CI2_I:K43A | null | null | null | -0.64 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":6.3,"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":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":29202,"numValue":-0.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29203,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7730,"numValue":7.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:6255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,255 | train | mutant | 87 | 95 | 97 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | P45A | P45A | 1 | 1 | 0 | 0 | 45 | P | A | 5 | CONSERVATION | null | false | false | null | null | 146 | ProTherm | 4.15 | CD | Thermal | acetate | 10 mM | null | 2CI2_I:P44A | 74.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":4.15,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2CI2_I:P44A","type":"_PDB... | [{"datasets":[],"id":574,"numValue":74.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":575,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":7731,"numValue":5.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:6256 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,256 | train | mutant | 87 | 95 | 97 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | P45A | P45A | 1 | 1 | 0 | 0 | 45 | P | A | 5 | CONSERVATION | null | false | false | null | null | 6,570 | ProTherm | 4.15 | CD | Thermal | acetate | 10 mM | 74.3 | 2CI2_I:P44A | null | null | null | -1.82 | null | null | null | null | null | null | null | null | null | null | null | null | no | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":4.15,"strValue":null,"type":"PH"},{"numValue":74.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CO... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":23491,"numValue":-1.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23492,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":7731,"numValue":5.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:6257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,257 | train | mutant | 87 | 95 | 97 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | P45A | P45A | 1 | 1 | 0 | 0 | 45 | P | A | 5 | CONSERVATION | null | false | false | null | null | 8,603 | ProTherm | 6.3 | DSC | GdnHCl | MES-NaOH | 50 mM | 25 | 2CI2_I:P44A | null | null | 5.23 | null | null | null | null | 2.96 | 1.95 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":6.3,"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":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":29198,"numValue":5.23,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29199,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29200,"numValue":2.96,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29201,"numValue":null,"references":[],"... | [{"id":7731,"numValue":5.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:6258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,258 | train | mutant | 87 | 95 | 97 | 84 | 84 | 10 | Hordeum vulgare | 1 | 10 | Hordeum vulgare | 1 | Q40059 | IPR000864|IPR036354 | P45A | P45A | 1 | 1 | 0 | 0 | 45 | P | A | 5 | CONSERVATION | null | false | false | null | null | 8,605 | ProTherm | 6.3 | DSC | GdnHCl | MES-NaOH | 50 mM | 25 | 2CI2_I:P44A | null | null | null | -1.93 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 12 | ARTICLE | Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2. | 1,994 | 10.1093/protein/7.1.103 | 7908135 | Protein Eng;7;103-8 | 3 | de Prat Gay G|Johnson C M|Fersht A R | [{"numValue":6.3,"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":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":29204,"numValue":-1.93,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29205,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7731,"numValue":5.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:6259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,259 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,696 | ProTherm | 7 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 51.5 | null | null | null | 79 | 2.2 | 112.3 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":65381,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65382,"numValue":79.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65383,"numValue":2.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65384,"numValue":112.3,"references":[]... | |||||||||||||||||||||||
fireprotdb:6260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,260 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,697 | ProTherm | 5 | DSC | Thermal | phosphate | 0.05 M | null | NaCl | 0.1 M | 47 | null | null | null | 53 | 2.2 | 88.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 16 | ARTICLE | Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. | 1,993 | 10.1002/pro.5560020408 | 8518730 | Protein Sci;2;567-76 | 3 | Tanaka A|Sturtevant J M|Flanagan J | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":65386,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65387,"numValue":53.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65388,"numValue":2.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65389,"numValue":88.2,"references":[],... | |||||||||||||||||||||||
fireprotdb:6261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,261 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,942 | ProTherm | 7 | CD | Thermal | cacodylate/pdTp | 10 mM/0.1 mM | null | CaCl2 | 10 mM | 52.5 | null | null | null | null | null | 73.9 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 894 | ARTICLE | Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant. | 1,991 | 10.1073/pnas.88.17.7715 | 1652762 | Proc Natl Acad Sci U S A;88;7715-8 | 5 | Nakano T|Kautz R A|Fox R O|Antonino L C|Fink A L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"cacodylate/pdTp","type":"BUFFER"},{"numValue":null,"strValue":"10 mM/0.1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"CaCl2","typ... | [{"datasets":[],"id":66353,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66354,"numValue":73.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66355,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,262 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,969 | ProTherm | 7 | DSC | Thermal | phosphate | 10 mM | null | NaCl | 0.1 M | 58.2 | null | null | null | 93 | 2 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1047 | ARTICLE | Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease. | 1,994 | 10.1002/pro.5560031203 | 7756977 | Protein Sci;3;2175-84 | 3 | Freire E|Xie D|Fox R | [{"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":66444,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66445,"numValue":93.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66446,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66447,"numValue":null,"references":[],... | |||||||||||||||||||||||
fireprotdb:6263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,263 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,970 | ProTherm | 4.1 | DSC | Thermal | acetate | 10 mM | null | NaCl | 0.1 M | 43.6 | null | null | null | 59 | 2.05 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1047 | ARTICLE | Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease. | 1,994 | 10.1002/pro.5560031203 | 7756977 | Protein Sci;3;2175-84 | 3 | Freire E|Xie D|Fox R | [{"numValue":4.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"num... | [{"datasets":[],"id":66448,"numValue":43.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66449,"numValue":59.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66450,"numValue":2.05,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66451,"numValue":null,"references":[]... | |||||||||||||||||||||||
fireprotdb:6264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,264 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,971 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 33.1 | null | null | null | 33 | 1.36 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1047 | ARTICLE | Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease. | 1,994 | 10.1002/pro.5560031203 | 7756977 | Protein Sci;3;2175-84 | 3 | Freire E|Xie D|Fox R | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{... | [{"datasets":[],"id":66452,"numValue":33.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66453,"numValue":33.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66454,"numValue":1.36,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66455,"numValue":null,"references":[]... | |||||||||||||||||||||||
fireprotdb:6265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,265 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,972 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.5 M | 33.9 | null | null | null | 38 | 1.05 | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DH|DCP|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1047 | ARTICLE | Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease. | 1,994 | 10.1002/pro.5560031203 | 7756977 | Protein Sci;3;2175-84 | 3 | Freire E|Xie D|Fox R | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{... | [{"datasets":[],"id":66456,"numValue":33.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66457,"numValue":38.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66458,"numValue":1.05,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66459,"numValue":3.0,"references":[],... | ||||||||||||||||||||||
fireprotdb:6266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,266 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,973 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.5 M | 60.4 | null | null | null | 21.5 | 0.51 | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | TM|DH|DCP|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1047 | ARTICLE | Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease. | 1,994 | 10.1002/pro.5560031203 | 7756977 | Protein Sci;3;2175-84 | 3 | Freire E|Xie D|Fox R | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{... | [{"datasets":[],"id":66461,"numValue":60.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66462,"numValue":21.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66463,"numValue":0.51,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66464,"numValue":3.0,"references":[],... | ||||||||||||||||||||||
fireprotdb:6267 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,267 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,285 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate,Sodium sulfate, | 10 mM,10 mM, | null | 53.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate,Sodium sulfate,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67473,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67474,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,268 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,290 | ProTherm | 7 | CD | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 54.1 | null | null | null | null | 2.15 | 77.5 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 266 | ARTICLE | Thermodynamics of staphylococcal nuclease denaturation. II. The A-state. | 1,994 | 10.1002/pro.5560030610 | 8069224 | Protein Sci;3;952-9 | 3 | Privalov P L|Carra J H|Anderson E A | [{"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":67485,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67486,"numValue":2.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67487,"numValue":77.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67488,"numValue":null,"references":... | |||||||||||||||||||||||
fireprotdb:6269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,269 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,291 | ProTherm | 4.1 | CD | Thermal | glycine-HCl | 20 mM | null | NaCl | 100 mM | 42.5 | null | null | null | null | 1.32 | 43.06 | null | null | null | null | null | null | null | null | null | yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 266 | ARTICLE | Thermodynamics of staphylococcal nuclease denaturation. II. The A-state. | 1,994 | 10.1002/pro.5560030610 | 8069224 | Protein Sci;3;952-9 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":4.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":67489,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67490,"numValue":1.32,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":67491,"numValue":43.06,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67492,"numValue":null,"references"... | |||||||||||||||||||||||
fireprotdb:6270 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,270 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,313 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 54.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 268 | ARTICLE | Energetics of denaturation and m values of staphylococcal nuclease mutants. | 1,995 | 10.1021/bi00006a025 | 7849061 | Biochemistry;34;2034-41 | 2 | Privalov P L|Carra J H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":67568,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67569,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,271 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,331 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 54.1 | null | null | null | 77.5 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 273 | ARTICLE | Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. | 1,994 | 10.1021/bi00201a035 | 8075087 | Biochemistry;33;10842-50 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":67652,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67653,"numValue":77.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67654,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,272 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,332 | ProTherm | 5 | DSC | Thermal | Sodium acetate | 20 mM | null | NaCl | 100 mM | 50.8 | null | null | null | 73.2 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 274 | ARTICLE | Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state. | 1,994 | 10.1002/pro.5560030609 | 8069223 | Protein Sci;3;944-51 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":67655,"numValue":50.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67656,"numValue":73.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67657,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,273 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,333 | ProTherm | 6 | DSC | Thermal | Sodium acetate | 20 mM | null | NaCl | 100 mM | 53.4 | null | null | null | 78.5 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 274 | ARTICLE | Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state. | 1,994 | 10.1002/pro.5560030609 | 8069223 | Protein Sci;3;944-51 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":67658,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67659,"numValue":78.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67660,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,274 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,334 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 54.1 | null | null | null | 77.5 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 274 | ARTICLE | Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state. | 1,994 | 10.1002/pro.5560030609 | 8069223 | Protein Sci;3;944-51 | 3 | Privalov P L|Carra J H|Anderson E A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":67661,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67662,"numValue":77.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67663,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,275 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,335 | ProTherm | 8 | DSC | Thermal | Sodium phosphate | 20 mM | null | NaCl | 100 mM | 53.5 | null | null | null | 83.7 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 274 | ARTICLE | Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state. | 1,994 | 10.1002/pro.5560030609 | 8069223 | Protein Sci;3;944-51 | 3 | Privalov P L|Carra J H|Anderson E A | [{"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":67664,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67665,"numValue":83.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":67666,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,276 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,517 | ProTherm | 7 | Fluorescence | Thermal | Tris-HCl | 0.01 M | null | NaCl | 0.1 M | 50.6 | null | null | null | null | null | 82.6 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 304 | ARTICLE | Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids. | 1,991 | 10.1021/bi00219a005 | 1991099 | Biochemistry;30;1193-9 | 4 | Eftink M R|Ghiron C A|Kautz R A|Fox R O | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":68302,"numValue":50.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68303,"numValue":82.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":68304,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,277 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,541 | ProTherm | 5.31 | NMR | Thermal | Unknown | null | NaCl | 0.3 M | 47.8 | null | null | null | null | null | 62.2 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.31,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.3 M","type":"ION_CONC"}] | [{"datasets":[],"id":68397,"numValue":47.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68398,"numValue":62.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":68399,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:6278 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,278 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,816 | ProTherm | 7 | CD | Thermal | PIPES | 0.05 mM | null | 53.1 | null | null | null | null | null | 78.7 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 320 | ARTICLE | Thermodynamics of the unfolding and spectroscopic properties of the V66W mutant of Staphylococcal nuclease and its 1-136 fragment. | 1,996 | 10.1021/bi9530090 | 8672513 | Biochemistry;35;8084-94 | 6 | Ionescu R|Eftink M R|Ramsay G D|Wong C Y|Wu J Q|Maki A H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69371,"numValue":53.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69372,"numValue":78.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":69373,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,279 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,940 | ProTherm | 7 | Fluorescence | Thermal | cacodylate | 10 mM | null | 53 | 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 | 1192 | ARTICLE | The folding of staphylococcal nuclease in the presence of methanol or guanidine thiocyanate. | 1,990 | 2373696 | J Biol Chem;265;12356-62 | 2 | Nakano T|Fink A L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":69877,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":69878,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":69879,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:6280 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,280 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,631 | ProTherm | 7 | Fluorescence | Thermal | NaOH | 25 mM | null | 53.5 | null | null | null | null | null | 86 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 382 | ARTICLE | The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability. | 1,996 | 10.1006/jmbi.1996.0180 | 8648619 | J Mol Biol;257;497-9 | 2 | Stites W E|Spencer D S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaOH","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72235,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72236,"numValue":86.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":72237,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,281 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,888 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 25 mM | null | NaCl | 100 mM | 53 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","... | [{"datasets":[],"id":73036,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73037,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,282 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,167 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 45 | null | null | 0.61 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":73898,"numValue":0.61,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73899,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,283 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,177 | ProTherm | 5.31 | NMR | Thermal | Unknown | 40 | NaCl | 0.3 M | null | null | 1.4 | null | null | 0 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 307 | ARTICLE | Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease. | 1,990 | 10.1021/bi00471a003 | 2372535 | Biochemistry;29;4516-25 | 3 | Alexandrescu A T|Hinck A P|Markley J L | [{"numValue":5.31,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":73929,"numValue":0.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73930,"numValue":1.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73931,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:6284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,284 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,179 | ProTherm | 5.5 | Fluorescence | Pressure | Bis-tris | 10 mM | 40 | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":[],"id":73936,"numValue":1.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73937,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,285 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,180 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 40 | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":73938,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73939,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,286 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,231 | ProTherm | 5.5 | NMR | Urea | succinate | 50 mM | 37 | null | null | 6.44 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1336 | ARTICLE | Hydrogen exchange in unligated and ligated staphylococcal nuclease. | 1,993 | 10.1021/bi00092a011 | 8218167 | Biochemistry;32;11022-8 | 4 | Wang J|Markley J L|Loh S N|Prehoda K E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":37.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"succinate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CON... | [{"datasets":[],"id":74095,"numValue":6.44,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74096,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,287 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,232 | ProTherm | 5.5 | Fluorescence | Urea | succinate | 50 mM | 37 | null | null | 6.13 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1336 | ARTICLE | Hydrogen exchange in unligated and ligated staphylococcal nuclease. | 1,993 | 10.1021/bi00092a011 | 8218167 | Biochemistry;32;11022-8 | 4 | Wang J|Markley J L|Loh S N|Prehoda K E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":37.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"succinate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":74097,"numValue":6.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74098,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,288 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,287 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 36 | null | null | 3.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":36.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":74252,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74253,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,289 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,312 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 25 mM | 35 | NaCl | 0.1 M | null | null | null | null | null | null | null | 0.61 | 5.88 | null | null | null | null | null | null | null | Unknown | M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1341 | ARTICLE | The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. | 1,999 | 10.1021/bi9909400 | 10460179 | Biochemistry;38;11216-22 | 3 | Yang M|Liu D|Bolen D W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":35.0,"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":"25 mM","type":... | [{"datasets":[],"id":74349,"numValue":5.88,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":74350,"numValue":0.61,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":74351,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,290 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,329 | ProTherm | 5.5 | Fluorescence | Pressure | Bis-tris | 10 mM | 30 | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":30.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":[],"id":74404,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74405,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,291 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,350 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 25 mM | 30 | NaCl | 0.1 M | null | null | null | null | null | null | null | 0.72 | 5.78 | null | null | null | null | null | null | null | Unknown | M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1341 | ARTICLE | The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. | 1,999 | 10.1021/bi9909400 | 10460179 | Biochemistry;38;11216-22 | 3 | Yang M|Liu D|Bolen D W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":30.0,"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":"25 mM","type":... | [{"datasets":[],"id":74462,"numValue":5.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":74463,"numValue":0.72,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":74464,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,292 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,637 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 25 | null | null | 4 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":75375,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75376,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,293 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,082 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 25 mM | 25 | NaCl | 0.1 M | null | null | null | null | null | null | null | 0.8 | 6 | null | null | null | null | null | null | null | Unknown | M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1341 | ARTICLE | The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. | 1,999 | 10.1021/bi9909400 | 10460179 | Biochemistry;38;11216-22 | 3 | Yang M|Liu D|Bolen D W | [{"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":"25 mM","type":... | [{"datasets":[],"id":76807,"numValue":6.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76808,"numValue":0.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76809,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,294 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,083 | ProTherm | 7 | DSC | GdnHCl | phosphate | 25 mM | 25 | NaCl | 0.1 M | null | null | null | null | null | null | null | 0.77 | 6.5 | null | null | null | null | null | null | null | Unknown | M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1341 | ARTICLE | The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. | 1,999 | 10.1021/bi9909400 | 10460179 | Biochemistry;38;11216-22 | 3 | Yang M|Liu D|Bolen D W | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_C... | [{"datasets":[],"id":76810,"numValue":6.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76811,"numValue":0.77,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76812,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,295 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,207 | ProTherm | 5.6 | Fluorescence | GdnHCl | Sodium acetate | 50 mM | 25 | NaCl | 100 mM | null | null | 3.8 | null | null | null | null | null | 5.9 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":5.6,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":77198,"numValue":3.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77199,"numValue":5.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77200,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,296 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,208 | ProTherm | 5.2 | Fluorescence | GdnHCl | Sodium acetate | 50 mM | 25 | NaCl | 100 mM | null | null | 4 | null | null | null | null | null | 5.5 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":5.2,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":77201,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77202,"numValue":5.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":77203,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,298 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,362 | ProTherm | 3 | DSC | Thermal | phosphate | 10 mM | 25 | null | null | 5.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1467 | ARTICLE | Least activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow circular dichroism. | 1,996 | 10.1073/pnas.93.6.2539 | 8637910 | Proc Natl Acad Sci U S A;93;2539-44 | 5 | Chen H M|Tsong T Y|Su Z D|Arooz M T|Gross C J | [{"numValue":3.0,"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":"10 mM","type":"BUFFER_... | [{"datasets":[],"id":77712,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77713,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,299 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,581 | ProTherm | 5.5 | Fluorescence | Pressure | Bis-tris | 10 mM | 21 | null | null | 3.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":21.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":[],"id":78375,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78376,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,300 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,591 | ProTherm | 7 | Fluorescence | Pressure | Bis-Tris | 10 mM | 21 | null | null | 3.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 817 | ARTICLE | Probing the contribution of internal cavities to the volume change of protein unfolding under pressure. | 1,998 | 10.1002/pro.5560071020 | 9792110 | Protein Sci;7;2217-22 | 2 | Royer C A|Frye K J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":21.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-Tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":[],"id":78397,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78398,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,302 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,646 | ProTherm | 8.8 | Fluorescence | GdnHCl | Tris-HCl | 25 mM | 20 | NaCl | 100 mM | null | null | 5.2 | null | null | null | null | 0.83 | 0.95 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 826 | ARTICLE | In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core. | 1,991 | 10.1016/0022-2836(91)80195-z | 1920420 | J Mol Biol;221;7-14 | 4 | Shortle D|Gittis A G|Stites W E|Lattman E E | [{"numValue":8.8,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"... | [{"datasets":[],"id":78555,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78556,"numValue":0.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78557,"numValue":0.83,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78558,"numValue":null,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:6303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,303 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,647 | ProTherm | 9.6 | Fluorescence | GdnHCl | ethanolamine-HCl | 25 mM | 20 | NaCl | 100 mM | null | null | 4.5 | null | null | null | null | 0.74 | 0.91 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 826 | ARTICLE | In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core. | 1,991 | 10.1016/0022-2836(91)80195-z | 1920420 | J Mol Biol;221;7-14 | 4 | Shortle D|Gittis A G|Stites W E|Lattman E E | [{"numValue":9.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"ethanolamine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":78559,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78560,"numValue":0.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78561,"numValue":0.74,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78562,"numValue":null,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:6304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,304 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,648 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.6 | 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 | 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":78563,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78564,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,305 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,661 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 20 | null | null | 4.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":78601,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78602,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,306 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,662 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.5 | null | null | null | null | 0.8 | 1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":78603,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78604,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78605,"numValue":0.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78606,"numValue":null,"references":[],"str... | |||||||||||||||||||||||
fireprotdb:6307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,307 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,669 | ProTherm | 7 | Fluorescence | GdnHCl | Na3PO4 | 25 mM | 20 | NaCl | 0.1 M | null | null | 5.6 | 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 | 837 | ARTICLE | Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction. | 1,988 | 10.1021/bi00413a027 | 3167015 | Biochemistry;27;4761-8 | 3 | Freire E|Shortle D|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Na3PO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BU... | [{"datasets":[],"id":78636,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78637,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,308 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,670 | ProTherm | 7 | Fluorescence | GdnHCl | Na2HPO4 | 25 mM | 20 | NaCl | 100 mM | null | null | 0 | null | null | null | null | null | 6.8 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 838 | ARTICLE | Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. | 1,990 | 10.1002/prot.340070402 | 2381904 | Proteins;7;299-305 | 2 | Shortle D|Sondek J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Na2HPO4","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"B... | [{"datasets":[],"id":78638,"numValue":0.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78639,"numValue":6.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78640,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,309 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,672 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5 | null | null | null | null | 0.84 | 1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 841 | ARTICLE | Stability studies of amino acid substitutions at tyrosine 27 of the staphylococcal nuclease beta-barrel. | 1,997 | 10.1021/bi970876r | 9315853 | Biochemistry;36;12167-74 | 5 | Fox R O|Bhat M G|Ganley L M|Ledman D W|Goodman M A | [{"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":78645,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78646,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78647,"numValue":0.84,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78648,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:6310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,310 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,673 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.33 | null | null | null | null | 0.79 | 6.72 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":78649,"numValue":5.33,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78650,"numValue":6.72,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78651,"numValue":0.79,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78652,"numValue":null,"references":[],"... | |||||||||||||||||||||||
fireprotdb:6311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,311 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,674 | ProTherm | 7 | CD | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.02 | null | null | null | null | 0.8 | 6.15 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 265 | ARTICLE | The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. | 1,993 | 10.1006/jmbi.1993.1425 | 8355268 | J Mol Biol;232;718-24 | 3 | Gittis A G|Stites W E|Lattman E E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BU... | [{"datasets":[],"id":78653,"numValue":5.02,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78654,"numValue":6.15,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78655,"numValue":0.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78656,"numValue":null,"references":[],"s... | |||||||||||||||||||||||
fireprotdb:6312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,312 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,675 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.6 | null | null | null | null | 0.82 | 1 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 843 | ARTICLE | Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. | 1,986 | 10.1002/prot.340010113 | 3449854 | Proteins;1;81-9 | 2 | Shortle D|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":78657,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78658,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78659,"numValue":0.82,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78660,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:6313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,313 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,676 | ProTherm | 7 | Fluorescence | Urea | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 6.1 | null | null | null | null | 2.56 | 1 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 843 | ARTICLE | Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. | 1,986 | 10.1002/prot.340010113 | 3449854 | Proteins;1;81-9 | 2 | Shortle D|Meeker A K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","t... | [{"datasets":[],"id":78661,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78662,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78663,"numValue":2.56,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78664,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:6314 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,314 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,680 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.5 | null | null | null | null | 0.83 | 1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":78675,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78676,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78677,"numValue":0.83,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78678,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:6316 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,316 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,708 | ProTherm | 7 | Fluorescence | GdnHCl | Potassium phosphate | 20 | NaCl | 100 mM | null | null | 5.5 | null | null | null | null | 0.85 | 1 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC | 851 | ARTICLE | Deletion of the omega-loop in the active site of staphylococcal nuclease. 1. Effect on catalysis and stability. | 1,991 | 10.1021/bi00229a005 | 2015219 | Biochemistry;30;3621-7 | 6 | Poole L B|Loveys D A|Hale S P|Gerlt J A|Stanczyk S M|Bolton P H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"NaCl... | [{"datasets":[],"id":78767,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78768,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78769,"numValue":0.85,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78770,"numValue":null,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:6317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,317 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,718 | ProTherm | 7 | CD | GdnHCl | PIPES | 0.05 mM | 20 | null | null | 5.32 | null | null | null | null | null | 5.83 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 320 | ARTICLE | Thermodynamics of the unfolding and spectroscopic properties of the V66W mutant of Staphylococcal nuclease and its 1-136 fragment. | 1,996 | 10.1021/bi9530090 | 8672513 | Biochemistry;35;8084-94 | 6 | Ionescu R|Eftink M R|Ramsay G D|Wong C Y|Wu J Q|Maki A H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"0.05 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":78800,"numValue":5.32,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78801,"numValue":5.83,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78802,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,319 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,746 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 25 mM | 20 | NaCl | 0.1 M | null | null | null | null | null | null | null | 0.84 | 5.72 | null | null | null | null | null | null | null | Unknown | M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1341 | ARTICLE | The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. | 1,999 | 10.1021/bi9909400 | 10460179 | Biochemistry;38;11216-22 | 3 | Yang M|Liu D|Bolen D W | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":... | [{"datasets":[],"id":78881,"numValue":5.72,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78882,"numValue":0.84,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78883,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,320 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,751 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.5 | null | null | null | null | null | 6.8 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 741 | ARTICLE | A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease. | 1,999 | 10.1038/12338 | 10467101 | Nat Struct Biol;6;876-83 | 2 | Wrabl J|Shortle D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":78900,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78901,"numValue":6.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78902,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,321 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,763 | ProTherm | 7 | Fluorescence | GdnHCl | NaOH | 25 mM | 20 | null | null | 5.5 | null | null | null | null | 0.83 | 6.6 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 382 | ARTICLE | The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability. | 1,996 | 10.1006/jmbi.1996.0180 | 8648619 | J Mol Biol;257;497-9 | 2 | Stites W E|Spencer D S | [{"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":"NaOH","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFF... | [{"datasets":[],"id":78929,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78930,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78931,"numValue":0.83,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78932,"numValue":null,"references":[],"st... | |||||||||||||||||||||||||
fireprotdb:6322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,322 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,794 | ProTherm | 7 | Fluorescence | GdnHCl | Tris-HCl | 0.01 M | 20 | NaCl | 0.1 M | null | null | 5.66 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 855 | ARTICLE | The use of fluorescence methods to monitor unfolding transitions in proteins. | 1,994 | 10.1016/s0006-3495(94)80799-4 | 8161701 | Biophys J;66;482-501 | 1 | Eftink M R | [{"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":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":... | [{"datasets":[],"id":79049,"numValue":5.66,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79050,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,323 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,795 | ProTherm | 7 | CD | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.4 | null | null | null | null | 0.8 | 1 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BU... | [{"datasets":[],"id":79051,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79052,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79053,"numValue":0.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79054,"numValue":null,"references":[],"str... | |||||||||||||||||||||||
fireprotdb:6324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,324 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,824 | ProTherm | 7 | Fluorescence | GdnHCl | Sodium phosphate | 25 mM | 20 | NaCl | 100 mM | null | null | 5.5 | null | null | null | null | 0.84 | 6.6 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 407 | ARTICLE | Chemically crosslinked protein dimers: stability and denaturation effects. | 1,995 | 10.1002/pro.5560041211 | 8580845 | Protein Sci;4;2545-58 | 2 | Stites W E|Byrne M P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"25 mM",... | [{"datasets":[],"id":79146,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79147,"numValue":6.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79148,"numValue":0.84,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79149,"numValue":null,"references":[],"st... | |||||||||||||||||||||||
fireprotdb:6325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,325 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,909 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 25 mM | 15.2 | NaCl | 0.1 M | null | null | null | null | null | null | null | 0.9 | 5.65 | null | null | null | null | null | null | null | Unknown | M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1341 | ARTICLE | The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. | 1,999 | 10.1021/bi9909400 | 10460179 | Biochemistry;38;11216-22 | 3 | Yang M|Liu D|Bolen D W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":15.2,"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":"25 mM","type":... | [{"datasets":[],"id":79386,"numValue":5.65,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79387,"numValue":0.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79388,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,326 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,912 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 15 | null | null | 4.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":15.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":79395,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79396,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,327 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,957 | ProTherm | 5.5 | Fluorescence | Pressure | Bis-tris | 10 mM | 10 | null | null | 3.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":[],"id":79540,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79541,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,328 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,958 | ProTherm | 5.5 | Absorbance | Pressure | Bis-tris | 50 mM | 10 | null | null | 4.15 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":79542,"numValue":4.15,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79543,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,330 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,040 | ProTherm | 7 | CD | Urea | Sodium cacodylate | 50 mM | 4.5 | NaCl | 50 mM | null | null | 3.7 | 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 | 1561 | ARTICLE | Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. | 1,991 | 10.1021/bi00224a018 | 2001357 | Biochemistry;30;2698-706 | 3 | Kuwajima K|Sugai S|Sugawara T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":4.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":79825,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79826,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,331 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,064 | ProTherm | 5.5 | Fluorescence | Pressure | Bis-tris | 10 mM | 2 | null | null | 2.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1331 | ARTICLE | Exploring the temperature-pressure phase diagram of staphylococcal nuclease. | 1,999 | 10.1021/bi982608e | 10194332 | Biochemistry;38;4157-64 | 6 | Panick G|Malessa R|Rapp G|Winter R|Vidugiris G J|Royer C A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":2.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Pressure","type":"METHOD"},{"numValue":null,"strValue":"Bis-tris","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":79897,"numValue":2.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79898,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:6333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,333 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,068 | ProTherm | 7 | CD | GdnSCN | cacodylate/pdTp | 10 mM/0.1 mM | 0 | CaCl2 | 10 mM | null | null | 4.6 | null | null | null | null | 0.3 | null | null | null | null | null | null | null | null | Unknown | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 894 | ARTICLE | Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant. | 1,991 | 10.1073/pnas.88.17.7715 | 1652762 | Proc Natl Acad Sci U S A;88;7715-8 | 5 | Nakano T|Kautz R A|Fox R O|Antonino L C|Fink A L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":0.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnSCN","type":"METHOD"},{"numValue":null,"strValue":"cacodylate/pdTp","type":"BUFFER"},{"numValue":null,"strValue":"10 mM/0.1 mM","type... | [{"datasets":[],"id":79907,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79908,"numValue":0.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79909,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:6334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6,334 | train | sequence | 117 | 117 | -1 | 231 | -1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | 11 | Thermonuclease | Staphylococcus aureus | 1 | P00644 | IPR035437|IPR016071|IPR002071 | 3.1.31.1 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,072 | ProTherm | 7 | Fluorescence | GdnSCN | cacodylate | 10 mM | 0 | null | null | 4.6 | null | null | null | null | 0.3 | 14 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 896 | ARTICLE | Effect of proline mutations on the stability and kinetics of folding of staphylococcal nuclease. | 1,993 | 10.1021/bi00061a010 | 8448112 | Biochemistry;32;2534-41 | 4 | Nakano T|Fox R O|Antonino L C|Fink A L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":0.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnSCN","type":"METHOD"},{"numValue":null,"strValue":"cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":79921,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79922,"numValue":14.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79923,"numValue":0.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79924,"numValue":null,"references":[],"st... |
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