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:17513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,513 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,991 | ProTherm | 7.5 | DSC | Thermal | imidazole | 50 mM | null | 51 | null | null | null | 25.1 | null | 45.41 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1051 | ARTICLE | Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. | 1,994 | 10.1002/pro.5560031127 | 7703860 | Protein Sci;3;2144-7 | 2 | Makhatadze G I|Marahiel M A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"imidazole","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66518,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66519,"numValue":25.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66520,"numValue":45.41,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66521,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:17514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,514 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,992 | ProTherm | 7.5 | DSC | Thermal | Sodium phosphate | 50 mM | null | 53.4 | null | null | null | 36.81 | null | 39.91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1051 | ARTICLE | Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. | 1,994 | 10.1002/pro.5560031127 | 7703860 | Protein Sci;3;2144-7 | 2 | Makhatadze G I|Marahiel M A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66522,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66523,"numValue":36.81,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66524,"numValue":39.91,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66525,"numValue":null,"references"... | |||||||||||||||||||||||||
fireprotdb:17516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,516 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,994 | ProTherm | 8 | DSC | Thermal | Sodium phosphate | 50 mM | null | 53.1 | null | null | null | 32.27 | null | 37.05 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1051 | ARTICLE | Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. | 1,994 | 10.1002/pro.5560031127 | 7703860 | Protein Sci;3;2144-7 | 2 | Makhatadze G I|Marahiel M A | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66530,"numValue":53.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66531,"numValue":32.27,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66532,"numValue":37.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66533,"numValue":null,"references"... | |||||||||||||||||||||||||
fireprotdb:17517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,517 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,995 | ProTherm | 9 | DSC | Thermal | glycine | 30 mM | null | 51 | null | null | null | 20.79 | null | 41.35 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1051 | ARTICLE | Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. | 1,994 | 10.1002/pro.5560031127 | 7703860 | Protein Sci;3;2144-7 | 2 | Makhatadze G I|Marahiel M A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66534,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66535,"numValue":20.79,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66536,"numValue":41.35,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66537,"numValue":null,"references"... | |||||||||||||||||||||||||
fireprotdb:17518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,518 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,996 | ProTherm | 9 | DSC | Thermal | glycine/sodium-phosphate | 30 mM/50 mM | null | 51.2 | null | null | null | 29.88 | null | 33.7 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1051 | ARTICLE | Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. | 1,994 | 10.1002/pro.5560031127 | 7703860 | Protein Sci;3;2144-7 | 2 | Makhatadze G I|Marahiel M A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine/sodium-phosphate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM/50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66538,"numValue":51.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66539,"numValue":29.88,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":66540,"numValue":33.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66541,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:17519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,519 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,193 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 47 | null | null | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67147,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67148,"numValue":39.91,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67149,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17521 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,521 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,195 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 48 | null | null | null | null | null | 43.98 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67153,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67154,"numValue":43.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67155,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,522 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,196 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 47.1 | null | null | null | null | null | 47.56 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67156,"numValue":47.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67157,"numValue":47.56,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67158,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,523 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,197 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 48.5 | null | null | null | null | null | 49.95 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67159,"numValue":48.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67160,"numValue":49.95,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67161,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,524 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,198 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 48.7 | null | null | null | null | null | 52.34 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67162,"numValue":48.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67163,"numValue":52.34,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67164,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,525 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,199 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 48.9 | null | null | null | null | null | 56.41 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67165,"numValue":48.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67166,"numValue":56.41,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67167,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,526 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,200 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 48.5 | null | null | null | null | null | 57.6 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67168,"numValue":48.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67169,"numValue":57.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67170,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,527 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,201 | ProTherm | 7 | Fluorescence | Thermal | sodium cacodylate-HCl | 10 mM | null | 48.9 | null | null | null | null | null | 60.71 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1063 | ARTICLE | Diffusional barrier crossing in a two-state protein folding reaction. | 1,999 | 10.1038/13289 | 10504725 | Nat Struct Biol;6;923-6 | 4 | Jacob M|Holtermann G|Geeves M|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67171,"numValue":48.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67172,"numValue":60.71,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":67173,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,528 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,408 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | null | 59.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":67904,"numValue":59.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67905,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,529 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,724 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | null | 53.6 | null | null | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":72537,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72538,"numValue":46.13,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":72539,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,530 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,731 | ProTherm | 7 | CD | Thermal | Sodium cacodylate | 5 M | null | 77.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1280 | ARTICLE | Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein. | 2,000 | 10.1006/jmbi.2000.3602 | 10736231 | J Mol Biol;297;975-88 | 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","type":"BUFFER"},{"numValue":null,"strValue":"5 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72552,"numValue":77.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72553,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,531 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,732 | ProTherm | 7 | CD | Thermal | Sodium cacodylate | 5 M | null | 49 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1280 | ARTICLE | Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein. | 2,000 | 10.1006/jmbi.2000.3602 | 10736231 | J Mol Biol;297;975-88 | 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","type":"BUFFER"},{"numValue":null,"strValue":"5 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72554,"numValue":49.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72555,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,532 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,132 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 70 | NaCl | 2 M | null | null | 0.19 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":73794,"numValue":0.19,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73795,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,533 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,164 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | null | null | 1.17 | null | null | 1.12 | 38.48 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"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":73886,"numValue":1.12,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73887,"numValue":38.48,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":73888,"numValue":1.17,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73889,"numValue":null,"references"... | |||||||||||||||||||||||||
fireprotdb:17535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,535 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,166 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | null | null | 15.39 | null | null | -0.02 | 32.74 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"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":73894,"numValue":-0.02,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73895,"numValue":32.74,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":73896,"numValue":15.39,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73897,"numValue":null,"reference... | |||||||||||||||||||||||||
fireprotdb:17536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,536 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,733 | ProTherm | 7 | CD | Urea | Potassium phosphate | 0.35 M | 25 | null | null | 3.49 | null | null | null | null | 4.45 | 0.78 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"... | [{"datasets":[],"id":75722,"numValue":3.49,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75723,"numValue":0.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75724,"numValue":4.45,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75725,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:17537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,537 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,867 | ProTherm | 7 | Absorbance | Thermal | Sodium cacodylate-HCl | 0.1 M | 25 | null | null | 2.13 | null | null | 0.91 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1408 | ARTICLE | Thermodynamic properties of an extremely rapid protein folding reaction. | 1,996 | 10.1021/bi962090j | 8988022 | Biochemistry;35;16833-42 | 2 | Schindler T|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1... | [{"datasets":[],"id":76169,"numValue":0.91,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":76170,"numValue":2.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76171,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,538 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,378 | ProTherm | 7 | CD | Urea | Sodium cacodylate-HCl | 0.1 M | 25 | null | null | 2.97 | null | null | null | null | null | null | null | null | null | null | null | null | null | Yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1470 | ARTICLE | Extremely rapid protein folding in the absence of intermediates. | 1,995 | 10.1038/nsb0895-663 | 7552728 | Nat Struct Biol;2;663-73 | 4 | Schindler T|Herrler M|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":... | [{"datasets":[],"id":77762,"numValue":2.97,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77763,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,539 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,338 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | null | 53.6 | null | null | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":80657,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80658,"numValue":46.13,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":80659,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,540 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,481 | ProTherm | 7 | CD | Thermal | sodium cacodylate | 100 mM | null | 53.6 | null | null | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1610 | ARTICLE | The effects of ionic strength on protein stability: the cold shock protein family. | 2,002 | 10.1016/S0022-2836(02)00259-0 | 12051927 | J Mol Biol;319;541-54 | 4 | Schmid Franz X|Brooks Charles L|Dominy Brian N|Perl Dieter | [{"numValue":7.0,"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":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":81071,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":81072,"numValue":46.13,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":81073,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,542 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,007 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 53.8 | null | null | null | null | null | 46.13 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":82643,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":82644,"numValue":46.13,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":82645,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,543 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,317 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 52.9 | null | null | null | 38.96 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":83550,"numValue":52.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83551,"numValue":38.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":83552,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,544 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,318 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 54.2 | null | null | null | null | null | 37.28 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":83553,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83554,"numValue":37.28,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83555,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,546 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,320 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 51 | null | null | null | null | null | 38 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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"}] | [{"datasets":[],"id":83559,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83560,"numValue":38.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83561,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,547 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,321 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 55.3 | null | null | null | null | null | 38.24 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83562,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83563,"numValue":38.24,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83564,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17548 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,548 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,322 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 49.7 | null | null | null | null | null | 34.66 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83565,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83566,"numValue":34.66,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83567,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,549 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,323 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 52.3 | null | null | null | null | null | 39.2 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83568,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83569,"numValue":39.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83570,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,550 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,324 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 56.4 | null | null | null | null | null | 39.2 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83571,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83572,"numValue":39.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83573,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,551 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,325 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 50.6 | null | null | null | null | null | 35.37 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83574,"numValue":50.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83575,"numValue":35.37,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83576,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,552 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,326 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 53.4 | null | null | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83577,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83578,"numValue":39.91,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83579,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,553 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,327 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 57.9 | null | null | null | null | null | 40.39 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83580,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83581,"numValue":40.39,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83582,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,554 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,328 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 53 | null | null | null | null | null | 37.28 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83583,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83584,"numValue":37.28,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83585,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,555 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,329 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 55.1 | null | null | null | null | null | 41.35 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83586,"numValue":55.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83587,"numValue":41.35,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83588,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,556 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,330 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 60.1 | null | null | null | null | null | 42.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83589,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83590,"numValue":42.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83591,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,558 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,332 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 58.7 | null | null | null | null | null | 44.46 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83595,"numValue":58.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83596,"numValue":44.46,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83597,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,559 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,333 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 64 | null | null | null | null | null | 45.41 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83598,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83599,"numValue":45.41,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83600,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,560 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,334 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 59.4 | null | null | null | null | null | 42.78 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83601,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83602,"numValue":42.78,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83603,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,561 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,335 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 63.1 | null | null | null | null | null | 48.04 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":[],"id":83604,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83605,"numValue":48.04,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83606,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,562 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,380 | ProTherm | 7 | CD | Thermal | Na cacodylate/HCl | 0.1 M | null | 53.8 | null | null | null | null | 0.96 | 46.13 | null | null | null | null | null | null | null | null | null | Yes | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 223 | ARTICLE | The correlation between protein stability and dipole moment: a critical test. | 2,006 | 10.1093/protein/gzl019 | 16720692 | Protein Eng Des Sel;19;355-8 | 2 | Wunderlich Michael|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":"Na cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":83732,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83733,"numValue":0.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":83734,"numValue":46.13,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":83735,"numValue":null,"references"... | |||||||||||||||||||||||||
fireprotdb:17563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,563 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,798 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 53.8 | null | null | null | 46.32 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":87651,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":87652,"numValue":46.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":87653,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":87654,"numValue":null,"references":... | ||||||||||||||||||||||
fireprotdb:17564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,564 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,799 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 53.8 | null | null | null | 46.32 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":87655,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":87656,"numValue":46.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":87657,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":87658,"numValue":null,"references":... | ||||||||||||||||||||||
fireprotdb:17565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,565 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,800 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 53.8 | null | null | null | 46.32 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":87659,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":87660,"numValue":46.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":87661,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":87662,"numValue":null,"references":... | ||||||||||||||||||||||
fireprotdb:17566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,566 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,133 | ProTherm | 7 | fluorescence | Urea | sodiumcacodylate | 20000.0 | null | null | null | 2.65 | null | null | null | null | 3.8 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88641,"numValue":2.65,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":88642,"numValue":3.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":88643,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":88644,"numValue":null,"references":[]... | ||||||||||||||||||||||||
fireprotdb:17568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,568 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,135 | ProTherm | 7 | fluorescence | Urea | sodiumcacodylate | 20000.0 | null | null | null | 2.51 | null | null | null | null | 3.6 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88649,"numValue":2.51,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":88650,"numValue":3.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":88651,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":88652,"numValue":null,"references":[]... | ||||||||||||||||||||||||
fireprotdb:17569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,569 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,136 | ProTherm | 7 | fluorescence | Urea | sodiumcacodylate | 20000.0 | null | null | null | 2.29 | null | null | null | null | 3.3 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88653,"numValue":2.29,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":88654,"numValue":3.3,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":88655,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":88656,"numValue":null,"references":[]... | ||||||||||||||||||||||||
fireprotdb:17571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,571 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,138 | ProTherm | 7 | fluorescence | Urea | sodiumcacodylate | 20000.0 | null | null | null | 2.15 | null | null | null | null | 3.1 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88661,"numValue":2.15,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":88662,"numValue":3.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":88663,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":88664,"numValue":null,"references":[]... | ||||||||||||||||||||||||
fireprotdb:17572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,572 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,139 | ProTherm | 7 | fluorescence | Urea | sodiumcacodylate | 20000.0 | null | null | null | 2.63 | null | null | null | null | 3.8 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88665,"numValue":2.63,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":88666,"numValue":3.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":88667,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":88668,"numValue":null,"references":[]... | ||||||||||||||||||||||||
fireprotdb:17573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,573 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,140 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 75.67 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88669,"numValue":75.67,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88670,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,574 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,141 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 75.38 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88671,"numValue":75.38,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88672,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,575 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,142 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 76.12 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88673,"numValue":76.12,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88674,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,576 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,143 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 76.07 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88675,"numValue":76.07,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88676,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,577 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,144 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 76.62 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88677,"numValue":76.62,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88678,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,578 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,145 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 75.74 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88679,"numValue":75.74,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88680,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,579 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,146 | ProTherm | 7 | spectroscopy | Thermal | sodiumcacodylate | 20000.0 | null | 75.62 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1789 | ARTICLE | What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein. | 2,020 | 10.1038/s41598-020-59446-w | 32060391 | Sci Rep;10;2640 | 5 | Welte Hannah|Zhou Tiankun|Mihajlenko Xenia|Mayans Olga|Kovermann Michael | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"spectroscopy","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodiumcacodylate","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"}] | [{"datasets":[],"id":88681,"numValue":75.62,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":88682,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,580 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,255 | ProTherm | 7 | CD | Thermal | Na cacodylate/HCl | 0.1 M | 75 | null | null | null | null | null | 0.96 | null | null | null | null | null | null | null | null | null | null | Yes | DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 223 | ARTICLE | The correlation between protein stability and dipole moment: a critical test. | 2,006 | 10.1093/protein/gzl019 | 16720692 | Protein Eng Des Sel;19;355-8 | 2 | Wunderlich Michael|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":75.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Na cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"... | [{"datasets":[],"id":89018,"numValue":0.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":89019,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,582 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,257 | ProTherm | 7 | CD | Thermal | Na cacodylate/HCl | 0.1 M | 75 | NaCl | 2 M | null | null | null | null | null | 0.96 | null | null | null | null | null | null | null | null | null | null | Yes | DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 223 | ARTICLE | The correlation between protein stability and dipole moment: a critical test. | 2,006 | 10.1093/protein/gzl019 | 16720692 | Protein Eng Des Sel;19;355-8 | 2 | Wunderlich Michael|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":75.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Na cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"... | [{"datasets":[],"id":89022,"numValue":0.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":89023,"numValue":null,"references":[],"strValue":"Yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,584 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,268 | ProTherm | 7 | CD | Thermal | sodium cacodylate | 100 mM | 60 | NaCl | 2 M | null | null | 1.43 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1610 | ARTICLE | The effects of ionic strength on protein stability: the cold shock protein family. | 2,002 | 10.1016/S0022-2836(02)00259-0 | 12051927 | J Mol Biol;319;541-54 | 4 | Schmid Franz X|Brooks Charles L|Dominy Brian N|Perl Dieter | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"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":"100 mM","type":... | [{"datasets":[],"id":89050,"numValue":1.43,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89051,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,585 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,277 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | null | null | 0.02 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89081,"numValue":0.02,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89082,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,586 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,278 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | null | null | 0.17 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89083,"numValue":0.17,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89084,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,587 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,279 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | null | null | 0.33 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89085,"numValue":0.33,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89086,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,588 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,280 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | null | null | 0.02 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89087,"numValue":0.02,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89088,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,589 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,281 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | null | null | 0.62 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89089,"numValue":0.62,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89090,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,592 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,284 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89095,"numValue":1.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89096,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,593 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,285 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | null | null | 0.55 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 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":89097,"numValue":0.55,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":89098,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:17595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,595 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 501,335 | MegaScale | null | null | null | null | 4.540137 | null | null | null | null | null | null | null | null | null | null | null | null | null | 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":2363891,"numValue":4.5401366041476745,"references":[],"strValue":null,"type":"DG"}] | ||||||||||||||||||||||||||||||||
fireprotdb:17596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,596 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 501,336 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | 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":2363894,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | |||||||||||||||||||||||||||||||
fireprotdb:17597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,597 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 501,337 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | 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":2363897,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | |||||||||||||||||||||||||||||||
fireprotdb:17598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,598 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 501,338 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | 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":2363900,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | |||||||||||||||||||||||||||||||
fireprotdb:17599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,599 | train | sequence | 358 | 358 | -1 | 67 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 501,339 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | 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":2363903,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | |||||||||||||||||||||||||||||||
fireprotdb:17600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,600 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 1,756 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R | 64.2 | 10.4 | null | null | null | null | 54.02 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|PON-TStab_dataset.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 | 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":["M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":6568,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv"],"id":6569,"numValue":10.4,"references":[],... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,601 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,331 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R | 64.2 | 10.4 | null | -1.75 | 54.24 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.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":19443,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19444,"numValue":10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19445,"numValue":54.24,"references":[],"strValue":null,"type":"DH"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":19... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,602 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,348 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R | 64.2 | 10.4 | null | -0.94 | 54.24 | 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":19545,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19546,"numValue":10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19547,"numValue":54.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19548,"numValue":-0.94,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,603 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,365 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R | 64.2 | 10.4 | null | -0.82 | 54.24 | 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":19647,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19648,"numValue":10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19649,"numValue":54.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19650,"numValue":-0.82,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,604 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,390 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R | null | 10.4 | null | -1.75 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | DTM|DDG|STATE|REVERSIBILITY | potapov_with_uniprot_mapping.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":19791,"numValue":10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":19792,"numValue":-1.75,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":19793,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id"... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:17605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,605 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,395 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R | null | 10.4 | null | -0.94 | 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":19811,"numValue":10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19812,"numValue":-0.94,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":19813,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":19814,"numValue":null,"references... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,606 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,400 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R | null | 10.4 | null | -0.82 | 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":19831,"numValue":10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19832,"numValue":-0.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":19833,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":19834,"numValue":null,"references... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,608 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,345 | 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":2363919,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363920,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363921,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,609 | train | mutant | 982 | 358 | 1,109 | 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 | M1R | M1R | 1 | 1 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,065,616 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.065321 | 0.046518 | 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":12123914,"numValue":-0.0653211287376226,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123915,"numValue":0.0465183664804885,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,610 | train | mutant | 7,437 | 358 | 8,120 | 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 | M1R|E3K | M1R|E3K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3 | A | L|E | false | false | 109.90048 | 29.098875 | 15,862 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R 1CSP_A:E3K | 77 | 23.2 | null | null | null | null | 62.62 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":58269,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58270,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58271,"numValue":62.62,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58272,"numValue":null,"references"... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,611 | train | mutant | 7,437 | 358 | 8,120 | 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 | M1R|E3K | M1R|E3K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3 | A | L|E | false | false | 109.90048 | 29.098875 | 16,494 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R 1CSP_A:E3K | 77 | 23.2 | null | -3.91 | 62.88 | 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":60391,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60392,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60393,"numValue":62.88,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60394,"numValue":-3.91,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,612 | train | mutant | 7,437 | 358 | 8,120 | 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 | M1R|E3K | M1R|E3K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3 | A | L|E | false | false | 109.90048 | 29.098875 | 16,530 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R 1CSP_A:E3K | 77 | 23.2 | null | -2.5 | 62.88 | 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":60607,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60608,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60609,"numValue":62.88,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60610,"numValue":-2.5,"references":[... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,613 | train | mutant | 7,437 | 358 | 8,120 | 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 | M1R|E3K | M1R|E3K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3 | A | L|E | false | false | 109.90048 | 29.098875 | 16,566 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:E3K | 77 | 23.2 | null | -1.42 | 62.88 | 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":60822,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60823,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60824,"numValue":62.88,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60825,"numValue":-1.42,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,614 | train | mutant | 7,437 | 358 | 8,120 | 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 | M1R|E3K | M1R|E3K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3 | A | L|E | false | false | 109.90048 | 29.098875 | 16,716 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:M1R 1CSP_A:E3K | null | null | null | -3.9 | 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":61495,"numValue":-3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61496,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,615 | train | mutant | 7,438 | 358 | 8,121 | 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 | M1R|E66K | M1R|E66K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|66 | A | L | false | false | 93.800578 | 41.934875 | 15,863 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R 1CSP_A:E66K | 69.5 | 15.7 | null | null | null | null | 52.34 | 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":58273,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58274,"numValue":15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58275,"numValue":52.34,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58276,"numValue":null,"references"... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,616 | train | mutant | 7,438 | 358 | 8,121 | 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 | M1R|E66K | M1R|E66K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|66 | A | L | false | false | 93.800578 | 41.934875 | 16,495 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R 1CSP_A:E66K | 69.5 | 15.7 | null | -2.64 | 52.56 | 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":60397,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60398,"numValue":15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60399,"numValue":52.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60400,"numValue":-2.64,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,617 | train | mutant | 7,438 | 358 | 8,121 | 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 | M1R|E66K | M1R|E66K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|66 | A | L | false | false | 93.800578 | 41.934875 | 16,531 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R 1CSP_A:E66K | 69.5 | 15.7 | null | -1.54 | 52.56 | 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":60613,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60614,"numValue":15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60615,"numValue":52.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60616,"numValue":-1.54,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,618 | train | mutant | 7,438 | 358 | 8,121 | 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 | M1R|E66K | M1R|E66K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|66 | A | L | false | false | 93.800578 | 41.934875 | 16,567 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:E66K | 69.5 | 15.7 | null | -1.1 | 52.56 | 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":60828,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60829,"numValue":15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60830,"numValue":52.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60831,"numValue":-1.1,"references":[... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,619 | train | mutant | 7,438 | 358 | 8,121 | 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 | M1R|E66K | M1R|E66K | 2 | 2 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|66 | A | L | false | false | 93.800578 | 41.934875 | 16,717 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:M1R 1CSP_A:E66K | null | null | null | -2.63 | 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":61497,"numValue":-2.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61498,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,620 | train | mutant | 7,439 | 358 | 8,122 | 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 | M1R|E3K|K65I | M1R|E3K|K65I | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65 | A | L|E | false | false | 104.945754 | 34.758509 | 15,864 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I | 83.7 | 29.9 | null | null | null | null | 66.44 | 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":58277,"numValue":83.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58278,"numValue":29.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58279,"numValue":66.44,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58280,"numValue":null,"references"... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... | |||||||||||
fireprotdb:17621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,621 | train | mutant | 7,439 | 358 | 8,122 | 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 | M1R|E3K|K65I | M1R|E3K|K65I | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65 | A | L|E | false | false | 104.945754 | 34.758509 | 16,496 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I | 83.7 | 29.9 | null | -5.02 | 66.72 | 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":60403,"numValue":83.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60404,"numValue":29.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60405,"numValue":66.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60406,"numValue":-5.02,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... | ||||||||||
fireprotdb:17622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,622 | train | mutant | 7,439 | 358 | 8,122 | 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 | M1R|E3K|K65I | M1R|E3K|K65I | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65 | A | L|E | false | false | 104.945754 | 34.758509 | 16,532 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I | 83.7 | 29.9 | null | -1.97 | 66.72 | 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":60619,"numValue":83.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60620,"numValue":29.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60621,"numValue":66.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60622,"numValue":-1.97,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... | ||||||||||
fireprotdb:17623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,623 | train | mutant | 7,439 | 358 | 8,122 | 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 | M1R|E3K|K65I | M1R|E3K|K65I | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65 | A | L|E | false | false | 104.945754 | 34.758509 | 16,568 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I | 83.7 | 29.9 | null | -3.05 | 66.72 | 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":60834,"numValue":83.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60835,"numValue":29.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60836,"numValue":66.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60837,"numValue":-3.05,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... | ||||||||||
fireprotdb:17624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,624 | train | mutant | 7,439 | 358 | 8,122 | 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 | M1R|E3K|K65I | M1R|E3K|K65I | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65 | A | L|E | false | false | 104.945754 | 34.758509 | 16,718 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I | null | null | null | -5 | 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":61499,"numValue":-5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61500,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... | |||||||||||||
fireprotdb:17625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,625 | train | mutant | 7,440 | 358 | 8,123 | 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 | M1R|E3K|E66K | M1R|E3K|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|66 | A | L|E | false | false | 88.531284 | 37.287917 | 15,865 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:E66K | 61.1 | 7.3 | null | null | null | null | 39.67 | 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":58281,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58282,"numValue":7.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58283,"numValue":39.67,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58284,"numValue":null,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... | |||||||||||
fireprotdb:17627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,627 | train | mutant | 7,440 | 358 | 8,123 | 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 | M1R|E3K|E66K | M1R|E3K|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|66 | A | L|E | false | false | 88.531284 | 37.287917 | 16,533 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:E66K | 61.1 | 7.3 | null | -0.86 | 39.84 | 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":60625,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60626,"numValue":7.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60627,"numValue":39.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60628,"numValue":-0.86,"references":[... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"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"... |
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