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:17746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,746 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,117 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R | 66.9 | null | null | null | null | null | 45.65 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7899,"numValue":66.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":790... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,747 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,160 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R | 69.9 | null | null | null | null | null | 49.95 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8028,"numValue":69.9,"references":[],"strValue":nu... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17748 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,748 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,161 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R | 71 | null | null | null | null | null | 49.24 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8031,"numValue":71.0,"references":[],"strValue":null,"type":"TM"},{"dat... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,749 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,162 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R | 66.2 | null | null | null | null | null | 44.93 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8034,"numValue":66.2,"references":[],"strValue":nu... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,750 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,206 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R | 69.7 | null | null | null | null | null | 49.95 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8166,"numValue":69.7... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,751 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,207 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R | 70.7 | null | null | null | null | null | 49 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8169,"numValue":70.7... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,752 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,208 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R | 66.5 | null | null | null | null | null | 45.17 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8172,"numValue":66.5... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,753 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,252 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R | 70 | null | null | null | null | null | 50.43 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":8304,"numValue":70.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8305,"numValue":50.43,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8306,"numValue":null,"reference... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,754 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,253 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R | 70.6 | null | null | null | null | null | 49 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":8307,"numValue":70.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8308,"numValue":49.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8309,"numValue":null,"references... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,755 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,254 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R | 66.2 | null | null | null | null | null | 44.93 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":8310,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8311,"numValue":44.93,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17756 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,756 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,298 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R | 72.2 | null | null | null | null | null | 52.1 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|EASE-MM_S543.csv|khan_protherm_data_mapped.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","EASE-MM_S543.csv","khan_protherm_data_mapped.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8442,"numValue":72.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","khan_protherm_data_mapped.csv","Saraboji_S2204... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,757 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,299 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R | 72.5 | null | null | null | null | null | 50.67 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|EASE-MM_S543.csv|khan_protherm_data_mapped.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","EASE-MM_S543.csv","khan_protherm_data_mapped.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8445,"numValue":72.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","khan_protherm_data_mapped.csv","Saraboji_S2204.csv","STRUM_Q342... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,758 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,300 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R | 67.7 | null | null | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|khan_protherm_data_mapped.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","khan_protherm_data_mapped.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8448,"numValue":67.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8449,"numValue":46.13,"references":[],"strValue":null,"type":"DHVH"},{"dat... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,759 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 4,185 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | null | 1CSP_A:E3R | 69.6 | 16 | null | null | null | null | 52.34 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 392 | ARTICLE | Two exposed amino acid residues confer thermostability on a cold shock protein. | 2,000 | 10.1038/75151 | 10802734 | Nat Struct Biol;7;380-3 | 4 | Perl D|Mueller U|Heinemann U|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R",... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":15522,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":15523,"numValue":16.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,760 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,335 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3R | 69.6 | 15.8 | null | -2.66 | 52.56 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|capriotti_S1615_map.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":19467,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19468,"numValue":15.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19469,"numValue":52.56,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,761 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,352 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3R | 69.6 | 15.8 | null | -1.9 | 52.56 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":19569,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19570,"numValue":15.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19571,"numValue":52.56,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17762 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,762 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,369 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3R | 69.6 | 15.8 | null | -0.77 | 52.56 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|capriotti_S1615_map.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":19671,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19672,"numValue":15.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19673,"numValue":52.56,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,763 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,391 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3R | null | 16 | null | -2.66 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|khan_protherm_data_mapped.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":19795,"numValue":16.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":19796,"numValue":-2.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,764 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,396 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3R | null | 16 | null | -1.9 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|khan_protherm_data_mapped.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":19815,"numValue":16.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":19816,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,765 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,401 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3R | null | 16 | null | -0.77 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|khan_protherm_data_mapped.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":19835,"numValue":16.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":19836,"numValue":-0.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,767 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 6,668 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 70 | NaCl | 2 M | 1CSP_A:E3R | null | null | 0.96 | -0.76 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 392 | ARTICLE | Two exposed amino acid residues confer thermostability on a cold shock protein. | 2,000 | 10.1038/75151 | 10802734 | Nat Struct Biol;7;380-3 | 4 | Perl D|Mueller U|Heinemann U|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":23765,"numValue":0.96,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":23766,"numValue":-0.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":23767,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,768 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,175 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3R | null | null | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25116,"numValue":1.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25117,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,769 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,179 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3R | null | null | 1.94 | -2.41 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25124,"numValue":1.94,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25125,"numValue":-2.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25126,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,770 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,180 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3R | null | null | 2.15 | -2.25 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25127,"numValue":2.15,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25128,"numValue":-2.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25129,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17771 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,771 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,181 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3R | null | null | 1.39 | -2.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25130,"numValue":1.39,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25131,"numValue":-2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25132,"numValue":null,"referenc... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,772 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,189 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:E3R | null | null | 1.94 | -2.27 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25154,"numValue":1.94,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25155,"numValue":-2.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25156,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,773 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,190 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:E3R | null | null | 2.06 | -2.03 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25157,"numValue":2.06,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25158,"numValue":-2.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25159,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,774 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,191 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:E3R | null | null | 1.41 | -2.01 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25160,"numValue":1.41,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25161,"numValue":-2.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25162,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,775 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,203 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:E3R | null | null | 1.89 | -2.08 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25196,"numValue":1.89,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25197,"numValue":-2.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25198,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17776 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,776 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,204 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:E3R | null | null | 1.98 | -1.82 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25199,"numValue":1.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25200,"numValue":-1.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,777 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,205 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:E3R | null | null | 1.34 | -1.84 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25202,"numValue":1.34,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25203,"numValue":-1.84,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25204,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,778 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,218 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:E3R | null | null | 1.86 | -1.84 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25241,"numValue":1.86,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25242,"numValue":-1.84,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25243,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,779 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,219 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:E3R | null | null | 1.94 | -1.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25244,"numValue":1.94,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25245,"numValue":-1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25246,"numValue":null,"referenc... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,780 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,220 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:E3R | null | null | 1.36 | -1.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25247,"numValue":1.36,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25248,"numValue":-1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25249,"numValue":null,"referenc... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,782 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,241 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:E3R | null | null | 1.91 | -1.29 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25310,"numValue":1.91,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25311,"numValue":-1.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25312,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,783 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,242 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:E3R | null | null | 1.34 | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25313,"numValue":1.34,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25314,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25315,"numValue":null,"referenc... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,784 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,270 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E3R | null | null | 2.22 | -1.15 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25397,"numValue":2.22,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25398,"numValue":-1.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25399,"numValue":null,"referen... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,785 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,271 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E3R | null | null | 2.2 | -1.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25400,"numValue":2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25401,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25402,"numValue":null,"reference... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,787 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 8,810 | ProTherm | 7 | CD | GdnHCl | sodium cacodylate-HCl | 100 mM | 25 | 1CSP_A:E3R | null | null | 0.02 | -0.88 | null | null | null | 2.02 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","typ... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":29804,"numValue":0.02,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":29805,"numValue":-0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":29806,"numV... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,788 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,388 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364048,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364049,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364050,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,789 | train | mutant | 323 | 358 | 359 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,597 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.011839 | 0.02992 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123876,"numValue":-0.0118394890846142,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123877,"numValue":0.0299201118161021,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,790 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 569 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | null | 1CSP_A:E3L | 62.7 | 9.1 | null | null | null | null | 47.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3L"... | [{"datasets":[],"id":2260,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2261,"numValue":9.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2262,"numValue":47.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,791 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,333 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3L | 63.1 | 9.3 | null | -1.63 | 49.92 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | capriotti_S1615_map.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19455,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19456,"numValue":9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19457,"numValue":49.92,"references":[],"strValue":null,"type":"DH"},{"datasets":["capriotti_S1615_map.csv"],"id":19458,"numVa... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,792 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,350 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3L | 63.1 | 9.3 | null | -1.18 | 49.92 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19557,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19558,"numValue":9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19559,"numValue":49.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19560,"numValue":-1.18,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,793 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,367 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3L | 63.1 | 9.3 | null | -0.46 | 49.92 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19659,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19660,"numValue":9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19661,"numValue":49.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19662,"numValue":-0.46,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,794 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 6,639 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | 70 | NaCl | 2 M | 1CSP_A:E3L | null | null | 0.6 | -0.41 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","ty... | [{"datasets":[],"id":23682,"numValue":0.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23683,"numValue":-0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23684,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,795 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,395 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.182105 | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364069,"numValue":2.182105364642191,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364070,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364071,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,796 | train | mutant | 324 | 358 | 360 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L | E3L | 1 | 1 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,592 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.005093 | 0.030601 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123866,"numValue":0.00509325583373764,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123867,"numValue":0.0306006600992044,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17797 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,797 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 1,757 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:E3K | 70.4 | 16.6 | null | null | null | null | 48.52 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.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|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.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","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,798 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,334 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3K | 70.4 | 16.6 | null | -2.76 | 48.72 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19461,"numValue":70.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19462,"numValue":16.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19463,"numValue":48.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19464,"numValue":-2.76,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,799 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,351 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3K | 70.4 | 16.6 | null | -2.02 | 48.72 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19563,"numValue":70.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19564,"numValue":16.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19565,"numValue":48.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19566,"numValue":-2.02,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17800 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,800 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,368 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3K | 70.4 | 16.6 | null | -0.74 | 48.72 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19665,"numValue":70.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19666,"numValue":16.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19667,"numValue":48.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19668,"numValue":-0.74,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,801 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 6,673 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:E3K | null | null | null | -2.75 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":23779,"numValue":-2.75,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23780,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,802 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,389 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364051,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364052,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364053,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,803 | train | mutant | 983 | 358 | 1,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K | E3K | 1 | 1 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,591 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.042917 | 0.049391 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123864,"numValue":-0.0429173045759014,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123865,"numValue":0.0493912964329483,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,804 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,061 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3Q | 60.5 | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3Q","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,805 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,073 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3Q | 62 | null | null | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3Q","typ... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7767,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,806 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,118 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3Q | 62.6 | null | null | null | null | null | 46.61 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["EASE-MM_S238.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7902,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7903,"numValue":46.61,"references":[],"strValue":null,"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17807 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,807 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,163 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3Q | 62.8 | null | null | null | null | null | 46.85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8037,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,808 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,209 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3Q | 63.3 | null | null | null | null | null | 47.32 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8175,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datas... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,809 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,255 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3Q | 65.4 | null | null | null | null | null | 49 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8313,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8314,"numValue":49.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8315,"numValue":null,"r... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,810 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,301 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3Q | 68.5 | null | null | null | null | null | 51.63 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv"],"id":8451,"numValue":68.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,811 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,176 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3Q | null | null | 0.72 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":25118,"numValue":0.72,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25119,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,812 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,182 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3Q | null | null | 0.91 | -1.39 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25133,"numValue":0.91,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25134,"numValue":-1.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25135,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,813 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,192 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:E3Q | null | null | 0.98 | -1.31 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25163,"numValue":0.98,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25164,"numValue":-1.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25165,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17814 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,814 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,206 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:E3Q | null | null | 1 | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25205,"numValue":1.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25206,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25207,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17815 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,815 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,221 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:E3Q | null | null | 1.08 | -1.05 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25250,"numValue":1.08,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25251,"numValue":-1.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25252,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,816 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,243 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:E3Q | null | null | 1.36 | -0.88 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25316,"numValue":1.36,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25317,"numValue":-0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25318,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,817 | train | mutant | 1,152 | 358 | 1,298 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3Q | E3Q | 1 | 1 | 0 | 0 | 3 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 7,273 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E3Q | null | null | 1.82 | -0.74 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25406,"numValue":1.82,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25407,"numValue":-0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25408,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,820 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,336 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3V | 64 | 10.2 | null | -1.78 | 49.2 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19473,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19474,"numValue":10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19475,"numValue":49.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19476,"numValue":-1.78,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,821 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,353 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3V | 64 | 10.2 | null | -1.1 | 49.2 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19575,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19576,"numValue":10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19577,"numValue":49.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19578,"numValue":-1.1,"references":[]... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17822 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,822 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,370 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3V | 64 | 10.2 | null | -0.67 | 49.2 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19677,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19678,"numValue":10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19679,"numValue":49.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19680,"numValue":-0.67,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17823 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,823 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,388 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3V | null | 10.2 | null | -1.78 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19783,"numValue":10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19784,"numValue":-1.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":19785,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":19786,"numValue":null,"references... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,824 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,393 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3V | null | 10.2 | null | -1.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19803,"numValue":10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19804,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":19805,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":19806,"numValue":null,"references"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17825 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,825 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,398 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3V | null | 10.2 | null | -0.67 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19823,"numValue":10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19824,"numValue":-0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":19825,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":19826,"numValue":null,"references... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,826 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,396 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364072,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364073,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364074,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,827 | train | mutant | 2,905 | 358 | 3,294 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V | E3V | 1 | 1 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,600 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.013478 | 0.032366 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123882,"numValue":-0.0134783594588611,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123883,"numValue":0.032366371189542,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17828 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,828 | train | mutant | 6,951 | 358 | 7,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|E66L | E3R|E66L | 2 | 2 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 14,809 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | null | 1CSP_A:E3R 1CSP_A:E66L | 74.6 | 21 | null | null | null | null | 54.73 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 392 | ARTICLE | Two exposed amino acid residues confer thermostability on a cold shock protein. | 2,000 | 10.1038/75151 | 10802734 | Nat Struct Biol;7;380-3 | 4 | Perl D|Mueller U|Heinemann U|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R 1... | [{"datasets":[],"id":54690,"numValue":74.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54691,"numValue":21.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54692,"numValue":54.73,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54693,"numValue":null,"references"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,832 | train | mutant | 6,951 | 358 | 7,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|E66L | E3R|E66L | 2 | 2 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,511 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3R 1CSP_A:E66L | 74.6 | 20.8 | null | -3.41 | 54.96 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60493,"numValue":74.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60494,"numValue":20.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60495,"numValue":54.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60496,"numValue":-3.41,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17834 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,834 | train | mutant | 6,951 | 358 | 7,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|E66L | E3R|E66L | 2 | 2 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,582 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3R 1CSP_A:E66L | 74.6 | 3.3 | null | -1.73 | 54.96 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60918,"numValue":74.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60919,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60920,"numValue":54.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60921,"numValue":-1.73,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,836 | train | mutant | 6,951 | 358 | 7,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|E66L | E3R|E66L | 2 | 2 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,707 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | 70 | NaCl | 2 M | 1CSP_A:E3R 1CSP_A:E66L | null | null | 1.91 | -1.72 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","ty... | [{"datasets":[],"id":61475,"numValue":1.91,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61476,"numValue":-1.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61477,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,837 | train | mutant | 6,951 | 358 | 7,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|E66L | E3R|E66L | 2 | 2 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,868 | ProTherm | 7 | CD | GdnHCl | sodium cacodylate-HCl | 100 mM | 25 | 1CSP_A:E3R 1CSP_A:E66L | null | null | 0.67 | -1.53 | null | null | null | 2.32 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","typ... | [{"datasets":[],"id":61981,"numValue":0.67,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61982,"numValue":-1.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61983,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":61984,"numValue":2.32,"references":[]... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,838 | train | mutant | 7,324 | 358 | 7,994 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|T64V|E66L | E3R|T64V|E66L | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|64|66 | A | E|L | false | false | 60.103441 | 37.395238 | 15,685 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | null | 1CSP_A:E3R 1CSP_A:T64V 1CSP_A:E66L | 76.8 | 23.2 | null | null | null | null | 54.97 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R ... | [{"datasets":[],"id":57563,"numValue":76.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57564,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57565,"numValue":54.97,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":57566,"numValue":null,"references"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | |||||||||||||
fireprotdb:17839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,839 | train | mutant | 7,324 | 358 | 7,994 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|T64V|E66L | E3R|T64V|E66L | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|64|66 | A | E|L | false | false | 60.103441 | 37.395238 | 16,701 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | 70 | 1CSP_A:E3R 1CSP_A:T64V 1CSP_A:E66L | null | null | 1 | -3.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","ty... | [{"datasets":[],"id":61457,"numValue":1.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61458,"numValue":-3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61459,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | |||||||||||||
fireprotdb:17840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,840 | train | mutant | 7,324 | 358 | 7,994 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|T64V|E66L | E3R|T64V|E66L | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|64|66 | A | E|L | false | false | 60.103441 | 37.395238 | 16,708 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | 70 | NaCl | 2 M | 1CSP_A:E3R 1CSP_A:T64V 1CSP_A:E66L | null | null | 2.1 | -1.91 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","ty... | [{"datasets":[],"id":61478,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61479,"numValue":-1.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61480,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,841 | train | mutant | 7,444 | 358 | 8,127 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|E66K | E3K|E66K | 2 | 2 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 15,869 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:E3K 1CSP_A:E66K | 64.6 | 12.8 | null | null | null | null | 47.32 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":58297,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58298,"numValue":12.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58299,"numValue":47.32,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58300,"numValue":null,"references"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,842 | train | mutant | 7,444 | 358 | 8,127 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|E66K | E3K|E66K | 2 | 2 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,504 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3K 1CSP_A:E66K | 64.6 | 10.8 | null | -1.92 | 47.52 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60451,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60452,"numValue":10.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60453,"numValue":47.52,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60454,"numValue":-1.92,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,843 | train | mutant | 7,444 | 358 | 8,127 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|E66K | E3K|E66K | 2 | 2 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,540 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3K 1CSP_A:E66K | 64.6 | 10.8 | null | -1.51 | 47.52 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60667,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60668,"numValue":10.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60669,"numValue":47.52,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60670,"numValue":-1.51,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,844 | train | mutant | 7,444 | 358 | 8,127 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|E66K | E3K|E66K | 2 | 2 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,576 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3K 1CSP_A:E66K | 64.6 | 10.8 | null | -0.41 | 47.52 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60882,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60883,"numValue":10.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60884,"numValue":47.52,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60885,"numValue":-0.41,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,845 | train | mutant | 7,444 | 358 | 8,127 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|E66K | E3K|E66K | 2 | 2 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,723 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:E3K 1CSP_A:E66K | null | null | null | -1.91 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":61509,"numValue":-1.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61510,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,846 | train | mutant | 7,445 | 358 | 8,128 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|K65I|E66K | E3K|K65I|E66K | 3 | 3 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|65|66 | A | E|L | false | false | 72.94063 | 42.579259 | 15,870 | ProTherm | null | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 71.8 | 18 | null | null | null | null | 48.04 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0-2 M","... | [{"datasets":[],"id":58301,"numValue":71.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58302,"numValue":18.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58303,"numValue":48.04,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58304,"numValue":null,"references"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,847 | train | mutant | 7,445 | 358 | 8,128 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|K65I|E66K | E3K|K65I|E66K | 3 | 3 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|65|66 | A | E|L | false | false | 72.94063 | 42.579259 | 16,514 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 71.8 | 18 | null | -2.95 | 48.24 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60511,"numValue":71.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60512,"numValue":18.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60513,"numValue":48.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60514,"numValue":-2.95,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17848 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,848 | train | mutant | 7,445 | 358 | 8,128 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|K65I|E66K | E3K|K65I|E66K | 3 | 3 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|65|66 | A | E|L | false | false | 72.94063 | 42.579259 | 16,550 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 71.8 | 18 | null | -1.37 | 48.24 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60726,"numValue":71.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60727,"numValue":18.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60728,"numValue":48.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60729,"numValue":-1.37,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,849 | train | mutant | 7,445 | 358 | 8,128 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|K65I|E66K | E3K|K65I|E66K | 3 | 3 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|65|66 | A | E|L | false | false | 72.94063 | 42.579259 | 16,585 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 71.8 | 19.4 | null | -1.58 | 48.24 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60936,"numValue":71.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60937,"numValue":19.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60938,"numValue":48.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60939,"numValue":-1.58,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,850 | train | mutant | 7,445 | 358 | 8,128 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3K|K65I|E66K | E3K|K65I|E66K | 3 | 3 | 0 | 0 | 3 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|65|66 | A | E|L | false | false | 72.94063 | 42.579259 | 16,608 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 71.8 | 18 | null | -1.58 | 48.24 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":61074,"numValue":71.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61075,"numValue":18.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61076,"numValue":48.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61077,"numValue":-1.58,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,852 | train | mutant | 7,446 | 358 | 8,129 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|A46K|S48R | E3R|A46K|S48R | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48 | A | E | false | false | 43.471651 | 27.822333 | 15,871 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R | 74.5 | 20.7 | null | null | null | null | 54.49 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":58305,"numValue":74.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58306,"numValue":20.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58307,"numValue":54.49,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58308,"numValue":null,"references"... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17853 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,853 | train | mutant | 7,446 | 358 | 8,129 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|A46K|S48R | E3R|A46K|S48R | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48 | A | E | false | false | 43.471651 | 27.822333 | 16,515 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R | 74.5 | 20.7 | null | -3.38 | 54.72 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60517,"numValue":74.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60518,"numValue":20.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60519,"numValue":54.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60520,"numValue":-3.38,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,854 | train | mutant | 7,446 | 358 | 8,129 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|A46K|S48R | E3R|A46K|S48R | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48 | A | E | false | false | 43.471651 | 27.822333 | 16,551 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R | 74.5 | 20.7 | null | -2.21 | 54.72 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60732,"numValue":74.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60733,"numValue":20.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60734,"numValue":54.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60735,"numValue":-2.21,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,856 | train | mutant | 7,446 | 358 | 8,129 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|A46K|S48R | E3R|A46K|S48R | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48 | A | E | false | false | 43.471651 | 27.822333 | 16,609 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R | 74.5 | 20.7 | null | -1.18 | 54.72 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":61080,"numValue":74.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61081,"numValue":20.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61082,"numValue":54.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61083,"numValue":-1.18,"references":... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,857 | train | mutant | 7,446 | 358 | 8,129 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3R|A46K|S48R | E3R|A46K|S48R | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48 | A | E | false | false | 43.471651 | 27.822333 | 16,725 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R | null | null | null | -3.37 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":61513,"numValue":-3.37,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61514,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... |
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