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:20399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,399 | train | mutant | 476,675 | 358 | 478,027 | 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 | Q45I | Q45I | 1 | 1 | 0 | 0 | 45 | Q | I | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,321 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.187159 | 1.576466 | 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":2366846,"numValue":2.187159324754539,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366847,"numValue":1.576465838370389,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366848,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20400 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,400 | train | mutant | 476,675 | 358 | 478,027 | 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 | Q45I | Q45I | 1 | 1 | 0 | 0 | 45 | Q | I | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,668 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.248534 | 0.120706 | 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":12122018,"numValue":-0.248533588225109,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122019,"numValue":0.120706360491497,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,401 | train | mutant | 476,676 | 358 | 478,028 | 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 | Q45W | Q45W | 1 | 1 | 0 | 0 | 45 | Q | W | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,322 | 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":2366849,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366850,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366851,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,402 | train | mutant | 476,676 | 358 | 478,028 | 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 | Q45W | Q45W | 1 | 1 | 0 | 0 | 45 | Q | W | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,065,117 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.217793 | 0.043987 | 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":12122916,"numValue":-0.217792501714159,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122917,"numValue":0.0439870232379184,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,403 | train | mutant | 476,677 | 358 | 478,029 | 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 | Q45Y | Q45Y | 1 | 1 | 0 | 0 | 45 | Q | Y | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,323 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.146247 | 1.340086 | 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":2366852,"numValue":2.1462473886172324,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366853,"numValue":1.3400863311253894,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366854,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20405 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,405 | train | mutant | 476,678 | 358 | 478,030 | 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 | Q45F | Q45F | 1 | 1 | 0 | 0 | 45 | Q | F | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,324 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.198947 | 1.42182 | 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":2366855,"numValue":2.198947074570202,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366856,"numValue":1.4218197049685033,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366857,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20406 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,406 | train | mutant | 476,678 | 358 | 478,030 | 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 | Q45F | Q45F | 1 | 1 | 0 | 0 | 45 | Q | F | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,665 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.516361 | 0.069053 | 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":12122012,"numValue":-0.516361072338892,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122013,"numValue":0.0690529935973039,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,407 | train | mutant | 476,679 | 358 | 478,031 | 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 | Q45P | Q45P | 1 | 1 | 0 | 0 | 45 | Q | P | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,325 | MegaScale | null | null | null | null | 1.784774 | null | null | null | null | null | null | 0.336559 | -0.759912 | 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":2366858,"numValue":0.3365591082441409,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366859,"numValue":-0.7599120445243495,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366860,"numValue":1.7847744159716186,"references":[],"strValue":null,"... | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20408 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,408 | train | mutant | 476,679 | 358 | 478,031 | 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 | Q45P | Q45P | 1 | 1 | 0 | 0 | 45 | Q | P | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,673 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.964354 | 0.129591 | 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":12122028,"numValue":-0.964354262685283,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122029,"numValue":0.129590792100031,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20409 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,409 | train | mutant | 476,680 | 358 | 478,032 | 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 | Q45C | Q45C | 1 | 1 | 0 | 0 | 45 | Q | C | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,326 | MegaScale | null | null | null | null | 4.556408 | null | null | null | null | null | null | 1.963419 | 1.034227 | 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":2366861,"numValue":1.963419310746343,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366862,"numValue":1.0342266497464176,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366863,"numValue":4.556407935692727,"references":[],"strValue":null,"typ... | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,410 | train | mutant | 476,680 | 358 | 478,032 | 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 | Q45C | Q45C | 1 | 1 | 0 | 0 | 45 | Q | C | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,662 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.107541 | 0.058617 | 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":12122006,"numValue":-0.107541054714902,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122007,"numValue":0.0586166768676943,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20412 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,412 | train | mutant | 476,682 | 358 | 478,034 | 67 | 66 | 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 | delQ45 | delQ45 | 1 | 0 | 1 | 0 | 45 | Q | - | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,329 | MegaScale | null | null | null | null | 2.034607 | null | null | null | null | null | null | 0.289613 | -0.530414 | 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":2366870,"numValue":0.2896125771914604,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366871,"numValue":-0.5304140420132926,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366872,"numValue":2.034607163174859,"references":[],"strValue":null,"t... | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20413 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,413 | train | mutant | 476,682 | 358 | 478,034 | 67 | 66 | 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 | delQ45 | delQ45 | 1 | 0 | 1 | 0 | 45 | Q | - | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,660 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.078208 | 0.133804 | 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":12122002,"numValue":-1.07820772841465,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122003,"numValue":0.13380395246221,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,414 | train | mutant | 325 | 358 | 361 | 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 | A46E | A46E | 1 | 1 | 0 | 0 | 46 | A | E | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 570 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | null | 1CSP_A:A46E | 48.6 | -5 | null | null | null | null | 39.67 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:A46E... | [{"datasets":[],"id":2264,"numValue":48.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2265,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2266,"numValue":39.67,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":2267,"numValue":null,"references":[],... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:20415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,415 | train | mutant | 325 | 358 | 361 | 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 | A46E | A46E | 1 | 1 | 0 | 0 | 46 | A | E | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,338 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:A46E | 48.6 | -5.2 | null | 0.6 | 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":19485,"numValue":48.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19486,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19487,"numValue":39.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19488,"numValue":0.6,"references":[]... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,418 | train | mutant | 325 | 358 | 361 | 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 | A46E | A46E | 1 | 1 | 0 | 0 | 46 | A | E | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 6,640 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | 70 | NaCl | 2 M | 1CSP_A:A46E | null | null | 0.22 | -0.02 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","ty... | [{"datasets":[],"id":23685,"numValue":0.22,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":23686,"numValue":-0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23687,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,420 | train | mutant | 325 | 358 | 361 | 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 | A46E | A46E | 1 | 1 | 0 | 0 | 46 | A | E | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,096 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.028082 | 0.075503 | 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":12122874,"numValue":-0.0280816022509442,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122875,"numValue":0.0755031629523538,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,421 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 1,761 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:A46K | 62.2 | 8.4 | null | null | null | null | 51.63 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":["EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,422 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,339 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:A46K | 62.2 | 8.4 | null | -1.42 | 51.84 | 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":19491,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19492,"numValue":8.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19493,"numValue":51.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19494,"numValue":-1.42,"references":[... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,423 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,356 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:A46K | 62.2 | 8.4 | null | -0.65 | 51.84 | 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":19593,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19594,"numValue":8.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19595,"numValue":51.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19596,"numValue":-0.65,"references":[... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,425 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,385 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46K | 62.2 | 8.4 | null | -0.77 | 51.84 | 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":19767,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19768,"numValue":8.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19769,"numValue":51.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19770,"numValue":-0.77,"references":[... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,426 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 6,677 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:A46K | null | null | null | -1.41 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23787,"numValue":-1.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23788,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,427 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,336 | 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":2366891,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366892,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366893,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,428 | train | mutant | 987 | 358 | 1,114 | 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 | A46K | A46K | 1 | 1 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,101 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.005249 | 0.059544 | 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":12122884,"numValue":0.00524904665524171,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122885,"numValue":0.0595439634644763,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,429 | train | mutant | 2,906 | 358 | 3,295 | 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 | A46L | A46L | 1 | 1 | 0 | 0 | 46 | A | L | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,340 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:A46L | 57.9 | 4.1 | null | -0.82 | 45.6 | 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":19497,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19498,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19499,"numValue":45.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19500,"numValue":-0.82,"references":[]... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,430 | train | mutant | 2,906 | 358 | 3,295 | 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 | A46L | A46L | 1 | 1 | 0 | 0 | 46 | A | L | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,357 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:A46L | 57.9 | 4.1 | null | -0.26 | 45.6 | 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":19599,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19600,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19601,"numValue":45.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19602,"numValue":-0.26,"references":[]... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,431 | train | mutant | 2,906 | 358 | 3,295 | 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 | A46L | A46L | 1 | 1 | 0 | 0 | 46 | A | L | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,374 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46L | 57.9 | 8.4 | null | -0.55 | 45.6 | 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":19701,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19702,"numValue":8.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19703,"numValue":45.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19704,"numValue":-0.55,"references":[]... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,432 | train | mutant | 2,906 | 358 | 3,295 | 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 | A46L | A46L | 1 | 1 | 0 | 0 | 46 | A | L | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,341 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.749098 | 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":2366906,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366907,"numValue":1.7490982233255326,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366908,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,433 | train | mutant | 2,906 | 358 | 3,295 | 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 | A46L | A46L | 1 | 1 | 0 | 0 | 46 | A | L | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,102 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.001606 | 0.034802 | 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":12122886,"numValue":0.00160636284062611,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122887,"numValue":0.0348015412005695,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20434 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,434 | train | mutant | 7,434 | 358 | 8,117 | 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 | A46K|S48R | A46K|S48R | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 15,859 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:A46K 1CSP_A:S48R | 69.7 | 15.9 | 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":58257,"numValue":69.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58258,"numValue":15.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58259,"numValue":52.34,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58260,"numValue":null,"references"... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,435 | train | mutant | 7,434 | 358 | 8,117 | 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 | A46K|S48R | A46K|S48R | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,525 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:A46K 1CSP_A:S48R | 69.7 | 15.9 | null | -2.66 | 52.56 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | 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":60577,"numValue":69.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60578,"numValue":15.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60579,"numValue":52.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60580,"numValue":-2.66,"references":... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,437 | train | mutant | 7,434 | 358 | 8,117 | 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 | A46K|S48R | A46K|S48R | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,596 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46K 1CSP_A:S48R | 69.7 | 13.8 | null | -1.2 | 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":61002,"numValue":69.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61003,"numValue":13.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61004,"numValue":52.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61005,"numValue":-1.2,"references":[... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,438 | train | mutant | 7,434 | 358 | 8,117 | 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 | A46K|S48R | A46K|S48R | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,605 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46K 1CSP_A:S48R | 69.7 | 15.9 | null | -1.2 | 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":61056,"numValue":69.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61057,"numValue":15.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61058,"numValue":52.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61059,"numValue":-1.2,"references":[... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,439 | train | mutant | 7,434 | 358 | 8,117 | 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 | A46K|S48R | A46K|S48R | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,713 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:A46K 1CSP_A:S48R | null | null | null | -2.65 | 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":61489,"numValue":-2.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61490,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:20440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,440 | train | mutant | 7,448 | 358 | 8,131 | 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 | A46K|S48R|E66L | A46K|S48R|E66L | 3 | 3 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48|66 | A | E|L | false | false | 32.738383 | 36.379667 | 15,873 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 77 | 23.2 | null | null | null | null | 55.21 | 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":58313,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58314,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58315,"numValue":55.21,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58316,"numValue":null,"references"... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:20441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,441 | train | mutant | 7,448 | 358 | 8,131 | 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 | A46K|S48R|E66L | A46K|S48R|E66L | 3 | 3 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48|66 | A | E|L | false | false | 32.738383 | 36.379667 | 16,526 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 77 | 23.2 | null | -3.77 | 55.44 | 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":60583,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60584,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60585,"numValue":55.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60586,"numValue":-3.77,"references":... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,443 | train | mutant | 7,448 | 358 | 8,131 | 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 | A46K|S48R|E66L | A46K|S48R|E66L | 3 | 3 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48|66 | A | E|L | false | false | 32.738383 | 36.379667 | 16,597 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 77 | 15.9 | null | -2.04 | 55.44 | 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":61008,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61009,"numValue":15.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61010,"numValue":55.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61011,"numValue":-2.04,"references":... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,444 | train | mutant | 7,448 | 358 | 8,131 | 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 | A46K|S48R|E66L | A46K|S48R|E66L | 3 | 3 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48|66 | A | E|L | false | false | 32.738383 | 36.379667 | 16,611 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 77 | 23.2 | null | -2.04 | 55.44 | 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":61092,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61093,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61094,"numValue":55.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61095,"numValue":-2.04,"references":... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,445 | train | mutant | 7,448 | 358 | 8,131 | 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 | A46K|S48R|E66L | A46K|S48R|E66L | 3 | 3 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48|66 | A | E|L | false | false | 32.738383 | 36.379667 | 16,727 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | null | null | null | -3.75 | 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":61517,"numValue":-3.75,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61518,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRang... | |||||||||||||
fireprotdb:20446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,446 | train | mutant | 7,843 | 358 | 8,555 | 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 | A46K|S48K | A46K|S48K | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,524 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:A46K 1CSP_A:S48K | 67.6 | 13.8 | null | -2.35 | 50.16 | 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":60571,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60572,"numValue":13.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60573,"numValue":50.16,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60574,"numValue":-2.35,"references":... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,447 | train | mutant | 7,843 | 358 | 8,555 | 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 | A46K|S48K | A46K|S48K | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,560 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:A46K 1CSP_A:S48K | 67.6 | 13.8 | null | -1.18 | 50.16 | 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":60786,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60787,"numValue":13.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60788,"numValue":50.16,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60789,"numValue":-1.18,"references":... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,448 | train | mutant | 7,843 | 358 | 8,555 | 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 | A46K|S48K | A46K|S48K | 2 | 2 | 0 | 0 | 46 | A | K | 2 | CONSERVATION | 1CSP | 247 | null | 46|48 | A | E | false | false | 26.211128 | 27.7365 | 16,595 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:A46K 1CSP_A:S48K | 67.6 | 4.1 | null | -1.18 | 50.16 | 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":60996,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60997,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60998,"numValue":50.16,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60999,"numValue":-1.18,"references":[... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20451 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,451 | train | mutant | 476,684 | 358 | 478,036 | 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 | A46N | A46N | 1 | 1 | 0 | 0 | 46 | A | N | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,332 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.237053 | 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":2366879,"numValue":2.237053489137298,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366880,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366881,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,452 | train | mutant | 476,684 | 358 | 478,036 | 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 | A46N | A46N | 1 | 1 | 0 | 0 | 46 | A | N | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,104 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.04723 | 0.066578 | 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":12122890,"numValue":-0.0472303796027371,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122891,"numValue":0.0665776982494939,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,453 | train | mutant | 476,685 | 358 | 478,037 | 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 | A46H | A46H | 1 | 1 | 0 | 0 | 46 | A | H | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,333 | 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":2366882,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366883,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366884,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20454 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,454 | train | mutant | 476,685 | 358 | 478,037 | 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 | A46H | A46H | 1 | 1 | 0 | 0 | 46 | A | H | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,099 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.017115 | 0.107625 | 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":12122880,"numValue":-0.0171149097765671,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122881,"numValue":0.107625022287594,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,455 | train | mutant | 476,686 | 358 | 478,038 | 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 | A46D | A46D | 1 | 1 | 0 | 0 | 46 | A | D | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,334 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.535996 | 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":2366885,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366886,"numValue":1.53599550284163,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366887,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,456 | train | mutant | 476,686 | 358 | 478,038 | 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 | A46D | A46D | 1 | 1 | 0 | 0 | 46 | A | D | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,095 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.082567 | 0.106873 | 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":12122872,"numValue":-0.0825666819983644,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122873,"numValue":0.106873423576291,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,457 | train | mutant | 476,687 | 358 | 478,039 | 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 | A46R | A46R | 1 | 1 | 0 | 0 | 46 | A | R | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,335 | 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":2366888,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366889,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366890,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,458 | train | mutant | 476,687 | 358 | 478,039 | 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 | A46R | A46R | 1 | 1 | 0 | 0 | 46 | A | R | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,107 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.007311 | 0.037786 | 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":12122896,"numValue":0.00731051496656063,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122897,"numValue":0.0377862786681946,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,459 | train | mutant | 476,688 | 358 | 478,040 | 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 | A46T | A46T | 1 | 1 | 0 | 0 | 46 | A | T | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,337 | 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":2366894,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366895,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366896,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,460 | train | mutant | 476,688 | 358 | 478,040 | 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 | A46T | A46T | 1 | 1 | 0 | 0 | 46 | A | T | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,109 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.052844 | 0.058463 | 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":12122900,"numValue":-0.0528437559744093,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122901,"numValue":0.0584631922410283,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,461 | train | mutant | 476,689 | 358 | 478,041 | 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 | A46S | A46S | 1 | 1 | 0 | 0 | 46 | A | S | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,338 | 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":2366897,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366898,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366899,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20462 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,462 | train | mutant | 476,689 | 358 | 478,041 | 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 | A46S | A46S | 1 | 1 | 0 | 0 | 46 | A | S | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,108 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.003394 | 0.040686 | 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":12122898,"numValue":0.00339427718977653,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122899,"numValue":0.040685564256875,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,463 | train | mutant | 476,690 | 358 | 478,042 | 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 | A46G | A46G | 1 | 1 | 0 | 0 | 46 | A | G | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,339 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.152994 | 1.582861 | 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":2366900,"numValue":2.152994367565607,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366901,"numValue":1.5828613691708977,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366902,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,464 | train | mutant | 476,690 | 358 | 478,042 | 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 | A46G | A46G | 1 | 1 | 0 | 0 | 46 | A | G | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,098 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.026947 | 0.043496 | 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":12122878,"numValue":-0.026946905322667,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122879,"numValue":0.0434955951985269,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20465 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,465 | train | mutant | 476,691 | 358 | 478,043 | 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 | A46M | A46M | 1 | 1 | 0 | 0 | 46 | A | M | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,340 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.217083 | 1.685926 | 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":2366903,"numValue":2.2170825115577277,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366904,"numValue":1.6859256689070266,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366905,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20466 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,466 | train | mutant | 476,691 | 358 | 478,043 | 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 | A46M | A46M | 1 | 1 | 0 | 0 | 46 | A | M | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,103 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.000531 | 0.053587 | 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":12122888,"numValue":-0.000530547482680933,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122889,"numValue":0.0535865837851318,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,467 | train | mutant | 476,692 | 358 | 478,044 | 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 | A46V | A46V | 1 | 1 | 0 | 0 | 46 | A | V | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,342 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.71693 | 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":2366909,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366910,"numValue":1.716929864548936,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366911,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,469 | train | mutant | 476,693 | 358 | 478,045 | 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 | A46I | A46I | 1 | 1 | 0 | 0 | 46 | A | I | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,343 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.729831 | 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":2366912,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366913,"numValue":1.7298306573624005,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366914,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,470 | train | mutant | 476,693 | 358 | 478,045 | 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 | A46I | A46I | 1 | 1 | 0 | 0 | 46 | A | I | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,100 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.027249 | 0.078512 | 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":12122882,"numValue":-0.0272492867203106,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122883,"numValue":0.0785115205165778,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20471 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,471 | train | mutant | 476,694 | 358 | 478,046 | 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 | A46W | A46W | 1 | 1 | 0 | 0 | 46 | A | W | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,344 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.846508 | 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":2366915,"numValue":1.8465084323177607,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366916,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366917,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,472 | train | mutant | 476,694 | 358 | 478,046 | 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 | A46W | A46W | 1 | 1 | 0 | 0 | 46 | A | W | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,111 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.049828 | 0.049064 | 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":12122904,"numValue":-0.0498279155439556,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122905,"numValue":0.0490640253048455,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20473 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,473 | train | mutant | 476,695 | 358 | 478,047 | 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 | A46Y | A46Y | 1 | 1 | 0 | 0 | 46 | A | Y | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,345 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.169539 | 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":2366918,"numValue":2.1695392957753894,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366919,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366920,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20474 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,474 | train | mutant | 476,695 | 358 | 478,047 | 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 | A46Y | A46Y | 1 | 1 | 0 | 0 | 46 | A | Y | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,112 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.013895 | 0.079849 | 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":12122906,"numValue":0.0138954372487145,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122907,"numValue":0.0798489908526867,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,475 | train | mutant | 476,696 | 358 | 478,048 | 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 | A46F | A46F | 1 | 1 | 0 | 0 | 46 | A | F | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,346 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.181399 | 1.636407 | 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":2366921,"numValue":2.181399248545844,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366922,"numValue":1.6364066867431126,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366923,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,476 | train | mutant | 476,696 | 358 | 478,048 | 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 | A46F | A46F | 1 | 1 | 0 | 0 | 46 | A | F | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,097 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.016753 | 0.060149 | 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":12122876,"numValue":-0.0167530334589003,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122877,"numValue":0.0601492230730132,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20478 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,478 | train | mutant | 476,697 | 358 | 478,049 | 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 | A46P | A46P | 1 | 1 | 0 | 0 | 46 | A | P | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,065,105 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.026069 | 0.057062 | 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":12122892,"numValue":-0.0260692019149022,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122893,"numValue":0.057061559393748,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,479 | train | mutant | 476,698 | 358 | 478,050 | 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 | A46C | A46C | 1 | 1 | 0 | 0 | 46 | A | C | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,348 | MegaScale | null | null | null | null | 4.706578 | null | null | null | null | null | null | 1.931142 | 1.138792 | 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":2366927,"numValue":1.9311417437749931,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366928,"numValue":1.1387922865686164,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366929,"numValue":4.706577607983757,"references":[],"strValue":null,"ty... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,481 | train | mutant | 476,699 | 358 | 478,051 | 67 | 68 | 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 | insG46 | insG46 | 1 | 0 | 0 | 1 | 46 | - | G | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,349 | MegaScale | null | null | null | null | 1.771725 | null | null | null | null | null | null | 0.200886 | -0.741311 | 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":2366930,"numValue":0.2008857725979305,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366931,"numValue":-0.7413113001597889,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366932,"numValue":1.771725420671843,"references":[],"strValue":null,"t... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,482 | train | mutant | 476,700 | 358 | 478,052 | 67 | 68 | 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 | insA46 | insA46 | 1 | 0 | 0 | 1 | 46 | - | A | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,350 | MegaScale | null | null | null | null | 1.561332 | null | null | null | null | null | null | 0.148547 | -0.942915 | 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":2366933,"numValue":0.14854696427744,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366934,"numValue":-0.9429153938975928,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366935,"numValue":1.5613318214630914,"references":[],"strValue":null,"ty... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20483 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,483 | train | mutant | 476,700 | 358 | 478,052 | 67 | 68 | 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 | insA46 | insA46 | 1 | 0 | 0 | 1 | 46 | - | A | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,372 | MegaScale | null | null | null | null | 1.52136 | null | null | null | null | null | null | 0.090347 | -0.93432 | 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":2366999,"numValue":0.0903469033466001,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367000,"numValue":-0.934319680031253,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367001,"numValue":1.5213598653646554,"references":[],"strValue":null,"t... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,484 | train | mutant | 476,701 | 358 | 478,053 | 67 | 66 | 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 | delA46 | delA46 | 1 | 0 | 1 | 0 | 46 | A | - | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 502,351 | MegaScale | null | null | null | null | 2.087176 | null | null | null | null | null | null | 0.410655 | -0.531045 | 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":2366936,"numValue":0.4106549174525067,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366937,"numValue":-0.5310453186165789,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366938,"numValue":2.087175812829871,"references":[],"strValue":null,"t... | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,485 | train | mutant | 476,701 | 358 | 478,053 | 67 | 66 | 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 | delA46 | delA46 | 1 | 0 | 1 | 0 | 46 | A | - | 2 | CONSERVATION | 1CSP | 247 | null | 46 | A | E | false | false | 23.831917 | 27.668 | 5,064,674 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.947482 | 0.089226 | 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":12122030,"numValue":-0.947481626036645,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122031,"numValue":0.0892255129182792,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,486 | train | mutant | 476,702 | 358 | 478,054 | 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 | V47Q | V47Q | 1 | 1 | 0 | 0 | 47 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,352 | MegaScale | null | null | null | null | 0.542672 | null | null | null | null | null | null | -0.481333 | -1.607171 | 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":2366939,"numValue":-0.4813328719660777,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366940,"numValue":-1.6071707700473723,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366941,"numValue":0.5426718118140927,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20488 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,488 | train | mutant | 476,703 | 358 | 478,055 | 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 | V47E | V47E | 1 | 1 | 0 | 0 | 47 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,353 | MegaScale | null | null | null | null | 0.315282 | null | null | null | null | null | null | -0.465211 | -1.713095 | 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":2366942,"numValue":-0.4652105972201286,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366943,"numValue":-1.7130947353515251,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366944,"numValue":0.3152821769472976,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,489 | train | mutant | 476,703 | 358 | 478,055 | 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 | V47E | V47E | 1 | 1 | 0 | 0 | 47 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,679 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.934323 | 0.100535 | 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":12122040,"numValue":-0.934322515091929,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122041,"numValue":0.10053531320978,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,490 | train | mutant | 476,704 | 358 | 478,056 | 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 | V47N | V47N | 1 | 1 | 0 | 0 | 47 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,354 | MegaScale | null | null | null | null | 0.461033 | null | null | null | null | null | null | -0.374809 | -1.488386 | 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":2366945,"numValue":-0.3748093490148418,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366946,"numValue":-1.4883857318357925,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366947,"numValue":0.4610329625113104,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,491 | train | mutant | 476,704 | 358 | 478,056 | 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 | V47N | V47N | 1 | 1 | 0 | 0 | 47 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,687 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.733217 | 0.421267 | 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":12122056,"numValue":-0.733216621065139,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122057,"numValue":0.421266906907563,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20492 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,492 | train | mutant | 476,705 | 358 | 478,057 | 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 | V47H | V47H | 1 | 1 | 0 | 0 | 47 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,355 | MegaScale | null | null | null | null | 0.775007 | null | null | null | null | null | null | -0.105116 | -1.495016 | 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":2366948,"numValue":-0.1051164047071337,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366949,"numValue":-1.4950160490189426,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366950,"numValue":0.7750065445590852,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,494 | train | mutant | 476,706 | 358 | 478,058 | 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 | V47D | V47D | 1 | 1 | 0 | 0 | 47 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,356 | MegaScale | null | null | null | null | 0.130172 | null | null | null | null | null | null | -0.588213 | -1.641789 | 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":2366951,"numValue":-0.5882129663431103,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366952,"numValue":-1.641789041676916,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366953,"numValue":0.1301718454742128,"references":[],"strValue":null,"... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,495 | train | mutant | 476,706 | 358 | 478,058 | 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 | V47D | V47D | 1 | 1 | 0 | 0 | 47 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,678 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.91846 | 0.116931 | 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":12122038,"numValue":-0.918460065384304,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122039,"numValue":0.11693143848351,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,496 | train | mutant | 476,707 | 358 | 478,059 | 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 | V47R | V47R | 1 | 1 | 0 | 0 | 47 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,357 | MegaScale | null | null | null | null | 0.687382 | null | null | null | null | null | null | -0.458806 | -1.731289 | 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":2366954,"numValue":-0.4588063954745505,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366955,"numValue":-1.7312893445922315,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366956,"numValue":0.6873818674655963,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,497 | train | mutant | 476,707 | 358 | 478,059 | 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 | V47R | V47R | 1 | 1 | 0 | 0 | 47 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,690 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.769923 | 0.039341 | 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":12122062,"numValue":-0.769922901330497,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122063,"numValue":0.0393408993288912,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,498 | train | mutant | 476,708 | 358 | 478,060 | 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 | V47K | V47K | 1 | 1 | 0 | 0 | 47 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,358 | MegaScale | null | null | null | null | 0.357785 | null | null | null | null | null | null | -0.660895 | -1.627326 | 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":2366957,"numValue":-0.6608945356810381,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366958,"numValue":-1.6273259545306449,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366959,"numValue":0.3577850278127107,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20499 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,499 | train | mutant | 476,708 | 358 | 478,060 | 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 | V47K | V47K | 1 | 1 | 0 | 0 | 47 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,684 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.83254 | 0.073752 | 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":12122050,"numValue":-0.832540384630365,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122051,"numValue":0.0737520495846611,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,500 | train | mutant | 476,709 | 358 | 478,061 | 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 | V47T | V47T | 1 | 1 | 0 | 0 | 47 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,359 | MegaScale | null | null | null | null | 3.67385 | null | null | null | null | null | null | 1.688681 | 0.580618 | 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":2366960,"numValue":1.6886813956182287,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366961,"numValue":0.5806183665083864,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366962,"numValue":3.673849958432749,"references":[],"strValue":null,"ty... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,501 | train | mutant | 476,709 | 358 | 478,061 | 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 | V47T | V47T | 1 | 1 | 0 | 0 | 47 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,692 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.582798 | 0.046122 | 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":12122066,"numValue":-0.582798436179094,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122067,"numValue":0.0461222836505568,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,502 | train | mutant | 476,710 | 358 | 478,062 | 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 | V47S | V47S | 1 | 1 | 0 | 0 | 47 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,360 | MegaScale | null | null | null | null | 1.541898 | null | null | null | null | null | null | 0.125631 | -1.026067 | 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":2366963,"numValue":0.1256307735024723,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366964,"numValue":-1.0260674434160288,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366965,"numValue":1.5418976601431824,"references":[],"strValue":null,"... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,503 | train | mutant | 476,710 | 358 | 478,062 | 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 | V47S | V47S | 1 | 1 | 0 | 0 | 47 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,691 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.93355 | 0.053345 | 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":12122064,"numValue":-0.933550123826102,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122065,"numValue":0.0533453901526584,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,504 | train | mutant | 476,711 | 358 | 478,063 | 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 | V47A | V47A | 1 | 1 | 0 | 0 | 47 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,361 | MegaScale | null | null | null | null | 3.281765 | null | null | null | null | null | null | 1.247217 | 0.393429 | 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":2366966,"numValue":1.2472167062680657,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366967,"numValue":0.393428611829925,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366968,"numValue":3.2817651453924306,"references":[],"strValue":null,"ty... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,505 | train | mutant | 476,711 | 358 | 478,063 | 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 | V47A | V47A | 1 | 1 | 0 | 0 | 47 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,676 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.652255 | 0.055702 | 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":12122034,"numValue":-0.652254523193297,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122035,"numValue":0.0557024316800513,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,506 | train | mutant | 476,712 | 358 | 478,064 | 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 | V47G | V47G | 1 | 1 | 0 | 0 | 47 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,362 | MegaScale | null | null | null | null | 0.748529 | null | null | null | null | null | null | -0.226226 | -1.482204 | 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":2366969,"numValue":-0.2262263142907375,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366970,"numValue":-1.4822044382499904,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366971,"numValue":0.7485285981951355,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,507 | train | mutant | 476,712 | 358 | 478,064 | 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 | V47G | V47G | 1 | 1 | 0 | 0 | 47 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,681 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.894291 | 0.074749 | 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":12122044,"numValue":-0.894290836807091,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122045,"numValue":0.0747491108422868,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,508 | train | mutant | 476,713 | 358 | 478,065 | 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 | V47M | V47M | 1 | 1 | 0 | 0 | 47 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,363 | MegaScale | null | null | null | null | 2.793235 | null | null | null | null | null | null | 1.030357 | -0.163708 | 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":2366972,"numValue":1.030356686258918,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366973,"numValue":-0.1637084022303452,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366974,"numValue":2.7932353763513724,"references":[],"strValue":null,"t... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,509 | train | mutant | 476,713 | 358 | 478,065 | 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 | V47M | V47M | 1 | 1 | 0 | 0 | 47 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,686 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.803662 | 0.069522 | 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":12122054,"numValue":-0.80366222513577,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122055,"numValue":0.0695215927611979,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,510 | train | mutant | 476,714 | 358 | 478,066 | 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 | V47L | V47L | 1 | 1 | 0 | 0 | 47 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,364 | MegaScale | null | null | null | null | 4.890084 | null | null | null | null | null | null | 2.090049 | 1.301193 | 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":2366975,"numValue":2.0900485639128843,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366976,"numValue":1.3011930627645485,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366977,"numValue":4.890084365490394,"references":[],"strValue":null,"ty... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20511 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,511 | train | mutant | 476,714 | 358 | 478,066 | 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 | V47L | V47L | 1 | 1 | 0 | 0 | 47 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,685 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.304612 | 0.032426 | 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":12122052,"numValue":-0.304611537119954,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122053,"numValue":0.0324258783765591,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20512 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,512 | train | mutant | 476,715 | 358 | 478,067 | 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 | V47I | V47I | 1 | 1 | 0 | 0 | 47 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,365 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.461249 | 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":2366978,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366979,"numValue":1.4612486506792894,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366980,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,513 | train | mutant | 476,715 | 358 | 478,067 | 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 | V47I | V47I | 1 | 1 | 0 | 0 | 47 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,683 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.162048 | 0.062888 | 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":12122048,"numValue":-0.162048215051196,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122049,"numValue":0.0628876025037671,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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