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:17972 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,972 | train | mutant | 475,797 | 358 | 477,169 | 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 | G4Q | G4Q | 1 | 1 | 0 | 0 | 4 | G | Q | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,406 | MegaScale | null | null | null | null | 1.61366 | null | null | null | null | null | null | 0.098979 | -0.938383 | 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":2364102,"numValue":0.0989789874050609,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364103,"numValue":-0.9383828236457664,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364104,"numValue":1.6136596468324556,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,973 | train | mutant | 475,797 | 358 | 477,169 | 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 | G4Q | G4Q | 1 | 1 | 0 | 0 | 4 | G | Q | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,580 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.398935 | 0.0474 | 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":12123842,"numValue":-0.398934905994653,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123843,"numValue":0.0473999462583001,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17974 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,974 | train | mutant | 475,798 | 358 | 477,170 | 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 | G4E | G4E | 1 | 1 | 0 | 0 | 4 | G | E | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,407 | MegaScale | null | null | null | null | 0.929043 | null | null | null | null | null | null | 0.111239 | -1.379661 | 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":2364105,"numValue":0.1112386643047876,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364106,"numValue":-1.3796607171561035,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364107,"numValue":0.9290434474203986,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,975 | train | mutant | 475,798 | 358 | 477,170 | 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 | G4E | G4E | 1 | 1 | 0 | 0 | 4 | G | E | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,064,312 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.880901 | 0.063793 | 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":12121306,"numValue":-0.880901167713542,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121307,"numValue":0.0637925999727796,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17978 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,978 | train | mutant | 475,800 | 358 | 477,172 | 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 | G4H | G4H | 1 | 1 | 0 | 0 | 4 | G | H | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,409 | MegaScale | null | null | null | null | 2.310026 | null | null | null | null | null | null | 0.719671 | -0.435021 | 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":2364111,"numValue":0.7196713212384616,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364112,"numValue":-0.4350213558829784,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364113,"numValue":2.310026309096137,"references":[],"strValue":null,"t... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,979 | train | mutant | 475,800 | 358 | 477,172 | 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 | G4H | G4H | 1 | 1 | 0 | 0 | 4 | G | H | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,573 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.769239 | 0.085803 | 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":12123828,"numValue":-0.769239323099921,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123829,"numValue":0.085802653632904,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17980 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,980 | train | mutant | 475,801 | 358 | 477,173 | 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 | G4D | G4D | 1 | 1 | 0 | 0 | 4 | G | D | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,410 | MegaScale | null | null | null | null | 0.611172 | null | null | null | null | null | null | -0.154437 | -1.562939 | 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":2364114,"numValue":-0.1544365394391959,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364115,"numValue":-1.5629392286244772,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364116,"numValue":0.6111715769357826,"references":[],"strValue":null,... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17981 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,981 | train | mutant | 475,801 | 358 | 477,173 | 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 | G4D | G4D | 1 | 1 | 0 | 0 | 4 | G | D | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,064,311 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.829517 | 0.065179 | 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":12121304,"numValue":-0.829516509318959,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121305,"numValue":0.0651791382841653,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17982 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,982 | train | mutant | 475,802 | 358 | 477,174 | 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 | G4R | G4R | 1 | 1 | 0 | 0 | 4 | G | R | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,411 | MegaScale | null | null | null | null | 1.90241 | null | null | null | null | null | null | 0.247738 | -0.895487 | 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":2364117,"numValue":0.2477380918027537,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364118,"numValue":-0.8954873971974939,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364119,"numValue":1.9024096390470144,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17983 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,983 | train | mutant | 475,802 | 358 | 477,174 | 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 | G4R | G4R | 1 | 1 | 0 | 0 | 4 | G | R | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,581 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.006207 | 0.067736 | 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":12123844,"numValue":-1.00620709887252,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123845,"numValue":0.0677363771506877,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17984 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,984 | train | mutant | 475,803 | 358 | 477,175 | 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 | G4K | G4K | 1 | 1 | 0 | 0 | 4 | G | K | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,412 | MegaScale | null | null | null | null | 2.016491 | null | null | null | null | null | null | 0.254487 | -0.625663 | 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":2364120,"numValue":0.2544868816571253,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364121,"numValue":-0.6256626718552891,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364122,"numValue":2.016490759568411,"references":[],"strValue":null,"t... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17985 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,985 | train | mutant | 475,803 | 358 | 477,175 | 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 | G4K | G4K | 1 | 1 | 0 | 0 | 4 | G | K | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,575 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.861245 | 0.080824 | 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":12123832,"numValue":-0.861244966162418,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123833,"numValue":0.0808239715214378,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17986 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,986 | train | mutant | 475,804 | 358 | 477,176 | 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 | G4T | G4T | 1 | 1 | 0 | 0 | 4 | G | T | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,413 | MegaScale | null | null | null | null | 1.636586 | null | null | null | null | null | null | 0.249456 | -0.879544 | 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":2364123,"numValue":0.2494558763825126,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364124,"numValue":-0.8795438509750454,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364125,"numValue":1.6365857935989363,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17987 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,987 | train | mutant | 475,804 | 358 | 477,176 | 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 | G4T | G4T | 1 | 1 | 0 | 0 | 4 | G | T | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,583 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.880025 | 0.088193 | 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":12123848,"numValue":-0.880024507000252,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123849,"numValue":0.0881930613834851,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17988 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,988 | train | mutant | 475,805 | 358 | 477,177 | 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 | G4S | G4S | 1 | 1 | 0 | 0 | 4 | G | S | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,414 | MegaScale | null | null | null | null | 3.349023 | null | null | null | null | null | null | 1.290335 | 0.377334 | 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":2364126,"numValue":1.2903348073684913,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364127,"numValue":0.3773343914195142,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364128,"numValue":3.349023108735521,"references":[],"strValue":null,"ty... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17989 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,989 | train | mutant | 475,805 | 358 | 477,177 | 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 | G4S | G4S | 1 | 1 | 0 | 0 | 4 | G | S | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,582 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.762405 | 0.041148 | 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":12123846,"numValue":-0.762404706158577,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123847,"numValue":0.0411481771277852,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17990 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,990 | train | mutant | 475,806 | 358 | 477,178 | 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 | G4A | G4A | 1 | 1 | 0 | 0 | 4 | G | A | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,415 | MegaScale | null | null | null | null | 4.027465 | null | null | null | null | null | null | 1.724088 | 0.865524 | 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":2364129,"numValue":1.7240881287479055,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364130,"numValue":0.8655236484237798,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364131,"numValue":4.027464739827068,"references":[],"strValue":null,"ty... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17991 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,991 | train | mutant | 475,806 | 358 | 477,178 | 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 | G4A | G4A | 1 | 1 | 0 | 0 | 4 | G | A | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,064,309 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.480353 | 0.03834 | 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":12121300,"numValue":-0.480352906691786,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121301,"numValue":0.0383399494342248,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17992 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,992 | train | mutant | 475,807 | 358 | 477,179 | 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 | G4M | G4M | 1 | 1 | 0 | 0 | 4 | G | M | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,416 | MegaScale | null | null | null | null | 1.743258 | null | null | null | null | null | null | 0.214271 | -0.917588 | 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":2364132,"numValue":0.21427112659592,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364133,"numValue":-0.9175879710743,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364134,"numValue":1.7432580511513414,"references":[],"strValue":null,"type"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17993 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,993 | train | mutant | 475,807 | 358 | 477,179 | 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 | G4M | G4M | 1 | 1 | 0 | 0 | 4 | G | M | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,577 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.593061 | 0.098721 | 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":12123836,"numValue":-0.593060696533403,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123837,"numValue":0.0987212701637944,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17994 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,994 | train | mutant | 475,808 | 358 | 477,180 | 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 | G4L | G4L | 1 | 1 | 0 | 0 | 4 | G | L | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,417 | MegaScale | null | null | null | null | 1.140941 | null | null | null | null | null | null | -0.084392 | -1.275856 | 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":2364135,"numValue":-0.0843916671241023,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364136,"numValue":-1.2758558953192671,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364137,"numValue":1.1409405262501489,"references":[],"strValue":null,... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17995 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,995 | train | mutant | 475,808 | 358 | 477,180 | 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 | G4L | G4L | 1 | 1 | 0 | 0 | 4 | G | L | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,576 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.996982 | 0.050265 | 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":12123834,"numValue":-0.996982135515566,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123835,"numValue":0.0502651234706662,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17996 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,996 | train | mutant | 475,809 | 358 | 477,181 | 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 | G4V | G4V | 1 | 1 | 0 | 0 | 4 | G | V | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,418 | MegaScale | null | null | null | null | 1.488453 | null | null | null | null | null | null | 0.03818 | -0.947252 | 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":2364138,"numValue":0.03818042266783,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364139,"numValue":-0.9472519142516582,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364140,"numValue":1.4884531712243796,"references":[],"strValue":null,"ty... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17998 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,998 | train | mutant | 475,810 | 358 | 477,182 | 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 | G4I | G4I | 1 | 1 | 0 | 0 | 4 | G | I | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,419 | MegaScale | null | null | null | null | 1.747485 | null | null | null | null | null | null | 0.17269 | -0.856473 | 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":2364141,"numValue":0.1726895590664053,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364142,"numValue":-0.8564728487717259,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364143,"numValue":1.7474847132098152,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17999 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,999 | train | mutant | 475,810 | 358 | 477,182 | 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 | G4I | G4I | 1 | 1 | 0 | 0 | 4 | G | I | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,574 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.131054 | 0.138225 | 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":12123830,"numValue":-1.13105428739714,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123831,"numValue":0.13822460902484,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18000 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,000 | train | mutant | 475,811 | 358 | 477,183 | 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 | G4W | G4W | 1 | 1 | 0 | 0 | 4 | G | W | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,420 | MegaScale | null | null | null | null | 2.240774 | null | null | null | null | null | null | 0.618077 | -0.756778 | 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":2364144,"numValue":0.6180773828424377,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364145,"numValue":-0.7567783440061469,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364146,"numValue":2.240773836336196,"references":[],"strValue":null,"t... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18001 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,001 | train | mutant | 475,811 | 358 | 477,183 | 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 | G4W | G4W | 1 | 1 | 0 | 0 | 4 | G | W | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,585 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.819727 | 0.064007 | 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":12123852,"numValue":-0.819726773566567,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123853,"numValue":0.0640070270247394,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18002 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,002 | train | mutant | 475,812 | 358 | 477,184 | 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 | G4Y | G4Y | 1 | 1 | 0 | 0 | 4 | G | Y | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,421 | MegaScale | null | null | null | null | 2.392261 | null | null | null | null | null | null | 0.795352 | -0.640389 | 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":2364147,"numValue":0.7953520071250477,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364148,"numValue":-0.6403890328309494,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364149,"numValue":2.392260646289245,"references":[],"strValue":null,"t... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18003 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,003 | train | mutant | 475,812 | 358 | 477,184 | 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 | G4Y | G4Y | 1 | 1 | 0 | 0 | 4 | G | Y | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,586 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.049978 | 0.147605 | 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":12123854,"numValue":-1.0499784683591,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123855,"numValue":0.147605117863423,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18004 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,004 | train | mutant | 475,813 | 358 | 477,185 | 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 | G4F | G4F | 1 | 1 | 0 | 0 | 4 | G | F | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,422 | MegaScale | null | null | null | null | 2.125725 | null | null | null | null | null | null | 0.551983 | -0.809502 | 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":2364150,"numValue":0.5519829192761689,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364151,"numValue":-0.8095023805061139,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364152,"numValue":2.125724815991507,"references":[],"strValue":null,"t... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18005 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,005 | train | mutant | 475,813 | 358 | 477,185 | 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 | G4F | G4F | 1 | 1 | 0 | 0 | 4 | G | F | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,064,313 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.180909 | 0.166894 | 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":12121308,"numValue":-1.18090933139793,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121309,"numValue":0.166894352294446,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18006 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,006 | train | mutant | 475,814 | 358 | 477,186 | 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 | G4P | G4P | 1 | 1 | 0 | 0 | 4 | G | P | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,423 | MegaScale | null | null | null | null | 1.794105 | null | null | null | null | null | null | 0.287697 | -0.833201 | 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":2364153,"numValue":0.2876966856571111,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364154,"numValue":-0.8332008020999264,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364155,"numValue":1.7941047328124635,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18007 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,007 | train | mutant | 475,814 | 358 | 477,186 | 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 | G4P | G4P | 1 | 1 | 0 | 0 | 4 | G | P | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,065,579 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.99761 | 0.078063 | 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":12123840,"numValue":-0.997609837589295,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123841,"numValue":0.0780627325477019,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18008 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,008 | train | mutant | 475,815 | 358 | 477,187 | 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 | G4C | G4C | 1 | 1 | 0 | 0 | 4 | G | C | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,424 | MegaScale | null | null | null | null | 2.89294 | null | null | null | null | null | null | 0.945924 | -0.034312 | 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":2364156,"numValue":0.9459242189561778,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364157,"numValue":-0.0343116554509791,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364158,"numValue":2.8929400955562485,"references":[],"strValue":null,"... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18010 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,010 | train | mutant | 475,816 | 358 | 477,188 | 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 | insG4 | insG4 | 1 | 0 | 0 | 1 | 4 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,425 | MegaScale | null | null | null | null | 4.394669 | null | null | null | null | null | null | 1.649332 | 1.020797 | 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":2364159,"numValue":1.649332042419974,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364160,"numValue":1.0207970447754768,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364161,"numValue":4.394668895762926,"references":[],"strValue":null,"typ... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18011 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,011 | train | mutant | 475,816 | 358 | 477,188 | 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 | insG4 | insG4 | 1 | 0 | 0 | 1 | 4 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,447 | MegaScale | null | null | null | null | 4.501676 | null | null | null | null | null | null | 1.784299 | 1.058996 | 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":2364225,"numValue":1.7842992113433414,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364226,"numValue":1.0589959715640842,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364227,"numValue":4.501676002122155,"references":[],"strValue":null,"ty... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18012 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,012 | train | mutant | 475,817 | 358 | 477,189 | 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 | insA4 | insA4 | 1 | 0 | 0 | 1 | 4 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,426 | MegaScale | null | null | null | null | 4.82011 | null | null | null | null | null | null | 1.85216 | 1.228415 | 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":2364162,"numValue":1.852159960471848,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364163,"numValue":1.2284146037472274,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364164,"numValue":4.820109671830972,"references":[],"strValue":null,"typ... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18013 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,013 | train | mutant | 475,818 | 358 | 477,190 | 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 | delG4 | delG4 | 1 | 0 | 1 | 0 | 4 | G | - | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 501,427 | MegaScale | null | null | null | null | 1.590717 | null | null | null | null | null | null | 0.080286 | -0.860157 | 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":2364165,"numValue":0.080285570441449,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364166,"numValue":-0.8601565938366167,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364167,"numValue":1.5907174075245518,"references":[],"strValue":null,"t... | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18014 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,014 | train | mutant | 475,818 | 358 | 477,190 | 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 | delG4 | delG4 | 1 | 0 | 1 | 0 | 4 | G | - | 9 | CONSERVATION | 1CSP | 247 | null | 4 | A | E | false | false | 13.503134 | 25.235 | 5,064,308 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.135184 | 0.149232 | 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":12121298,"numValue":-1.13518403220135,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121299,"numValue":0.149231721243851,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20812,"numValue":9.0,"position":4,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18015 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,015 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,062 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K5Q | 33.4 | null | null | null | 23.66 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:K5Q","ty... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7734,"numValue":33.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18016 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,016 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,075 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K5Q | 34.9 | null | null | null | null | null | 26.77 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:K5Q","typ... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7773,"numValue":34.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18017 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,017 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,076 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K5Q | 31.2 | null | null | null | null | null | 22.47 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:K5Q","typ... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7776,"numValue":31.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18018 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,018 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,120 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:K5Q | 38.6 | null | null | null | null | null | 29.88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7908,"numValue":38.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7909,"numValue":29.88,"references":[],"strValue":null,"type":"DHVH"},{"... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18019 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,019 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,121 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:K5Q | 37.6 | null | null | null | null | null | 27.72 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7911,"numValue":37.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7912,"numValue":27.72,"references":[],"strValu... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18020 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,020 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,166 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:K5Q | 40.8 | null | null | null | null | null | 31.79 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8046,"numValue":40.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18021 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,021 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,167 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:K5Q | 39.5 | null | null | null | null | null | 29.4 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8049,"numValue":39.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18022 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,022 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,212 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:K5Q | 44.5 | null | null | null | null | null | 34.89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8184,"numValue":44.5,"references":[],"strValue":null... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18023 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,023 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,213 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:K5Q | 41.3 | null | null | null | null | null | 30.83 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S499.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8187,"numValue":41.3,"references":[],"strValue":null,"type":"TM"},{"da... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18024 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,024 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,258 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K5Q | 51.1 | null | null | null | null | null | 40.39 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8322,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8323,"numValue":40.39,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8324,"numValue":null,"references":[],"strValue":"Unknown... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18025 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,025 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,259 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K5Q | 48 | null | null | null | null | null | 36.57 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8325,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8326,"numValue":36.57,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8327,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18026 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,026 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,304 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K5Q | 57.7 | null | null | null | null | null | 45.89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv"],"id":8460,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"d... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18027 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,027 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,305 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K5Q | 54.7 | null | null | null | null | null | 42.07 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv"],"id":8463,"numValue":54.7,"references":[],"strValue":null,"type":"TM"},{"d... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18028 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,028 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 7,274 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:K5Q | null | null | 0.36 | 0.74 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25409,"numValue":0.36,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25410,"numValue":0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25411,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18029 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,029 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,428 | MegaScale | null | null | null | null | 4.78518 | null | null | null | null | null | null | 2.102241 | 1.213573 | 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":2364168,"numValue":2.102240746808382,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364169,"numValue":1.213572717274065,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364170,"numValue":4.785179659178262,"references":[],"strValue":null,"type... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18030 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,030 | train | mutant | 1,153 | 358 | 1,299 | 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 | K5Q | K5Q | 1 | 1 | 0 | 0 | 5 | K | Q | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,566 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.042308 | 0.038461 | 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":12123814,"numValue":-0.0423082483327775,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123815,"numValue":0.0384611105321772,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18031 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,031 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,074 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K5E | 8.1 | null | null | null | null | null | 2.87 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:K5E","typ... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7770,"numValue":8.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18033 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,033 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,164 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:K5E | 26.4 | null | null | null | null | null | 18.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8040,"numValue":26.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18035 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,035 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,210 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:K5E | 34.1 | null | null | null | null | null | 24.62 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8178,"numValue":34.1,"references":[],"strValue":null... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18036 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,036 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,211 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:K5E | 30 | null | null | null | null | null | 19.84 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv|Saraboji_S1396.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8181,"numValue":30.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18037 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,037 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,256 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K5E | 43.9 | null | null | null | null | null | 32.74 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8316,"numValue":43.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8317,"numValue":32.74,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8318,"numValue":null,"... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18038 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,038 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,257 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K5E | 41.9 | null | null | null | null | null | 29.88 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8319,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8320,"numValue":29.88,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8321,"numValue":null,"... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18039 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,039 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,302 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K5E | 53.5 | null | null | null | null | null | 40.87 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|EASE-MM_S1676.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv"],"id":8454,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S167... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18040 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,040 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 2,303 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K5E | 50.9 | null | null | null | null | null | 37.52 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv"],"id":8457,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18041 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,041 | train | mutant | 1,161 | 358 | 1,307 | 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 | K5E | K5E | 1 | 1 | 0 | 0 | 5 | K | E | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,429 | MegaScale | null | null | null | null | 4.330676 | null | null | null | null | null | null | 2.03027 | 1.039917 | 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":2364171,"numValue":2.0302700744841617,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364172,"numValue":1.0399174471510892,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364173,"numValue":4.330675851337254,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18043 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,043 | train | mutant | 475,819 | 358 | 477,191 | 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 | K5N | K5N | 1 | 1 | 0 | 0 | 5 | K | N | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,430 | MegaScale | null | null | null | null | 4.587371 | null | null | null | null | null | null | 2.20732 | 1.167216 | 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":2364174,"numValue":2.2073195989707486,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364175,"numValue":1.1672157544358706,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364176,"numValue":4.587370892071903,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18044 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,044 | train | mutant | 475,819 | 358 | 477,191 | 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 | K5N | K5N | 1 | 1 | 0 | 0 | 5 | K | N | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,564 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.113132 | 0.055795 | 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":12123810,"numValue":-0.113131737148009,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123811,"numValue":0.0557947040075594,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18045 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,045 | train | mutant | 475,820 | 358 | 477,192 | 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 | K5H | K5H | 1 | 1 | 0 | 0 | 5 | K | H | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,431 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.166109 | 1.561114 | 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":2364177,"numValue":2.1661093786849577,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364178,"numValue":1.561114147746185,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364179,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18047 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,047 | train | mutant | 475,821 | 358 | 477,193 | 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 | K5D | K5D | 1 | 1 | 0 | 0 | 5 | K | D | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,432 | MegaScale | null | null | null | null | 3.544252 | null | null | null | null | null | null | 1.700692 | 0.603601 | 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":2364180,"numValue":1.7006924466890123,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364181,"numValue":0.6036008519113415,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364182,"numValue":3.544251564213181,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18048 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,048 | train | mutant | 475,821 | 358 | 477,193 | 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 | K5D | K5D | 1 | 1 | 0 | 0 | 5 | K | D | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,317 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.599271 | 0.072883 | 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":12121316,"numValue":-0.599271168829225,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121317,"numValue":0.0728829944075389,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18049 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,049 | train | mutant | 475,822 | 358 | 477,194 | 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 | K5R | K5R | 1 | 1 | 0 | 0 | 5 | K | R | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,433 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.642465 | 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":2364183,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364184,"numValue":1.642464984374401,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364185,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18050 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,050 | train | mutant | 475,822 | 358 | 477,194 | 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 | K5R | K5R | 1 | 1 | 0 | 0 | 5 | K | R | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,567 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.031032 | 0.028502 | 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":12123816,"numValue":-0.0310324276141562,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123817,"numValue":0.0285023356049557,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18052 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,052 | train | mutant | 475,823 | 358 | 477,195 | 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 | K5T | K5T | 1 | 1 | 0 | 0 | 5 | K | T | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,569 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.008685 | 0.038525 | 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":12123820,"numValue":-0.0086850316240034,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123821,"numValue":0.038524629026173,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18053 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,053 | train | mutant | 475,824 | 358 | 477,196 | 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 | K5S | K5S | 1 | 1 | 0 | 0 | 5 | K | S | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,435 | MegaScale | null | null | null | null | 4.667753 | null | null | null | null | null | null | 2.1399 | 1.157226 | 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":2364189,"numValue":2.139899961459698,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364190,"numValue":1.1572260515690498,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364191,"numValue":4.667753188622191,"references":[],"strValue":null,"typ... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18054 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,054 | train | mutant | 475,824 | 358 | 477,196 | 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 | K5S | K5S | 1 | 1 | 0 | 0 | 5 | K | S | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,568 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.053563 | 0.028648 | 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":12123818,"numValue":-0.0535626018122152,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123819,"numValue":0.0286481410934909,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18055 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,055 | train | mutant | 475,825 | 358 | 477,197 | 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 | K5A | K5A | 1 | 1 | 0 | 0 | 5 | K | A | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,436 | MegaScale | null | null | null | null | 4.499401 | null | null | null | null | null | null | 2.154891 | 0.944642 | 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":2364192,"numValue":2.154891092191737,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364193,"numValue":0.9446419534040646,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364194,"numValue":4.49940102194775,"references":[],"strValue":null,"type... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18056 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,056 | train | mutant | 475,825 | 358 | 477,197 | 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 | K5A | K5A | 1 | 1 | 0 | 0 | 5 | K | A | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,315 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.166344 | 0.034036 | 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":12121312,"numValue":-0.166344116286685,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121313,"numValue":0.034036252524164,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18057 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,057 | train | mutant | 475,826 | 358 | 477,198 | 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 | K5G | K5G | 1 | 1 | 0 | 0 | 5 | K | G | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,437 | MegaScale | null | null | null | null | 3.505376 | null | null | null | null | null | null | 1.920972 | 0.256374 | 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":2364195,"numValue":1.920971616458245,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364196,"numValue":0.2563735362675553,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364197,"numValue":3.5053756975882573,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18058 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,058 | train | mutant | 475,826 | 358 | 477,198 | 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 | K5G | K5G | 1 | 1 | 0 | 0 | 5 | K | G | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,320 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.679151 | 0.049157 | 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":12121322,"numValue":-0.679150643161553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121323,"numValue":0.0491570152514921,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18059 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,059 | train | mutant | 475,827 | 358 | 477,199 | 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 | K5M | K5M | 1 | 1 | 0 | 0 | 5 | K | M | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,438 | MegaScale | null | null | null | null | 4.733174 | null | null | null | null | null | null | 2.076975 | 1.216746 | 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":2364198,"numValue":2.076974954153302,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364199,"numValue":1.2167461432259157,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364200,"numValue":4.733174068003384,"references":[],"strValue":null,"typ... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18060 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,060 | train | mutant | 475,827 | 358 | 477,199 | 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 | K5M | K5M | 1 | 1 | 0 | 0 | 5 | K | M | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,563 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.083616 | 0.045386 | 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":12123808,"numValue":-0.0836161233195982,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123809,"numValue":0.0453862394874163,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18061 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,061 | train | mutant | 475,828 | 358 | 477,200 | 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 | K5L | K5L | 1 | 1 | 0 | 0 | 5 | K | L | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,439 | MegaScale | null | null | null | null | 4.631961 | null | null | null | null | null | null | 2.041353 | 1.197919 | 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":2364201,"numValue":2.041352899519449,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364202,"numValue":1.1979185006724955,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364203,"numValue":4.631960819363462,"references":[],"strValue":null,"typ... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18062 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,062 | train | mutant | 475,828 | 358 | 477,200 | 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 | K5L | K5L | 1 | 1 | 0 | 0 | 5 | K | L | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,562 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.116103 | 0.027635 | 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":12123806,"numValue":-0.116103416400713,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123807,"numValue":0.0276354516857395,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18063 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,063 | train | mutant | 475,829 | 358 | 477,201 | 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 | K5V | K5V | 1 | 1 | 0 | 0 | 5 | K | V | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,440 | MegaScale | null | null | null | null | 4.917808 | null | null | null | null | null | null | 2.168262 | 1.318604 | 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":2364204,"numValue":2.168262107218081,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364205,"numValue":1.3186043696250016,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364206,"numValue":4.917807680321548,"references":[],"strValue":null,"typ... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18064 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,064 | train | mutant | 475,829 | 358 | 477,201 | 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 | K5V | K5V | 1 | 1 | 0 | 0 | 5 | K | V | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,570 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.083368 | 0.028635 | 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":12123822,"numValue":-0.0833677166947591,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123823,"numValue":0.0286354508883849,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18065 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,065 | train | mutant | 475,830 | 358 | 477,202 | 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 | K5I | K5I | 1 | 1 | 0 | 0 | 5 | K | I | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,441 | MegaScale | null | null | null | null | 4.911931 | null | null | null | null | null | null | 2.133471 | 1.250465 | 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":2364207,"numValue":2.133471314215158,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364208,"numValue":1.2504646345156685,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364209,"numValue":4.91193117266711,"references":[],"strValue":null,"type... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18066 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,066 | train | mutant | 475,830 | 358 | 477,202 | 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 | K5I | K5I | 1 | 1 | 0 | 0 | 5 | K | I | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,322 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.056868 | 0.043933 | 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":12121326,"numValue":-0.0568679432968024,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121327,"numValue":0.0439333060719841,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18068 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,068 | train | mutant | 475,831 | 358 | 477,203 | 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 | K5W | K5W | 1 | 1 | 0 | 0 | 5 | K | W | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,571 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.155687 | 0.036317 | 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":12123824,"numValue":-0.155686552056552,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123825,"numValue":0.0363172938913499,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18069 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,069 | train | mutant | 475,832 | 358 | 477,204 | 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 | K5Y | K5Y | 1 | 1 | 0 | 0 | 5 | K | Y | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,443 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.115876 | 1.416388 | 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":2364213,"numValue":2.115875611795423,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364214,"numValue":1.416388205856762,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364215,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18070 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,070 | train | mutant | 475,832 | 358 | 477,204 | 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 | K5Y | K5Y | 1 | 1 | 0 | 0 | 5 | K | Y | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,572 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.038567 | 0.052964 | 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":12123826,"numValue":-0.0385674285676082,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123827,"numValue":0.0529636535719983,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18071 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,071 | train | mutant | 475,833 | 358 | 477,205 | 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 | K5F | K5F | 1 | 1 | 0 | 0 | 5 | K | F | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,444 | MegaScale | null | null | null | null | 4.859924 | null | null | null | null | null | null | 2.021845 | 1.259057 | 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":2364216,"numValue":2.0218448301018226,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364217,"numValue":1.2590570190181551,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364218,"numValue":4.859923539109525,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18072 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,072 | train | mutant | 475,833 | 358 | 477,205 | 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 | K5F | K5F | 1 | 1 | 0 | 0 | 5 | K | F | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,319 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.061529 | 0.043752 | 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":12121320,"numValue":-0.0615287875984127,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121321,"numValue":0.0437515705585524,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18074 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,074 | train | mutant | 475,834 | 358 | 477,206 | 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 | K5P | K5P | 1 | 1 | 0 | 0 | 5 | K | P | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,065,565 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.922567 | 0.073257 | 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":12123812,"numValue":-0.922567054914977,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123813,"numValue":0.0732567697092103,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18075 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,075 | train | mutant | 475,835 | 358 | 477,207 | 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 | K5C | K5C | 1 | 1 | 0 | 0 | 5 | K | C | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,446 | MegaScale | null | null | null | null | 4.693838 | null | null | null | null | null | null | 1.920963 | 1.116158 | 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":2364222,"numValue":1.9209630058307297,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364223,"numValue":1.1161578659778075,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364224,"numValue":4.693838147589744,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18076 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,076 | train | mutant | 475,835 | 358 | 477,207 | 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 | K5C | K5C | 1 | 1 | 0 | 0 | 5 | K | C | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,316 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.052149 | 0.052571 | 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":12121314,"numValue":-0.0521488307745508,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121315,"numValue":0.0525707294929751,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18077 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,077 | train | mutant | 475,836 | 358 | 477,208 | 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 | insA5 | insA5 | 1 | 0 | 0 | 1 | 5 | - | A | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,448 | MegaScale | null | null | null | null | 3.220859 | null | null | null | null | null | null | 1.136715 | 0.286894 | 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":2364228,"numValue":1.1367154081491635,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364229,"numValue":0.2868939681741759,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364230,"numValue":3.220858652682293,"references":[],"strValue":null,"ty... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18078 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,078 | train | mutant | 475,837 | 358 | 477,209 | 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 | delK5 | delK5 | 1 | 0 | 1 | 0 | 5 | K | - | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 501,449 | MegaScale | null | null | null | null | 0.177655 | null | null | null | null | null | null | -0.547343 | -1.853584 | 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":2364231,"numValue":-0.5473433883626024,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364232,"numValue":-1.8535838351429272,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364233,"numValue":0.177655320499605,"references":[],"strValue":null,"... | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18079 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,079 | train | mutant | 475,837 | 358 | 477,209 | 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 | delK5 | delK5 | 1 | 0 | 1 | 0 | 5 | K | - | 6 | CONSERVATION | 1CSP | 247 | null | 5 | A | E | false | false | 97.928725 | 38.081111 | 5,064,314 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.118751 | 0.12006 | 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":12121310,"numValue":-1.11875059073242,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121311,"numValue":0.120059583242379,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18080 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,080 | train | mutant | 475,838 | 358 | 477,210 | 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 | V6Q | V6Q | 1 | 1 | 0 | 0 | 6 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 6 | A | E | false | false | 1.970407 | 21.922857 | 501,450 | MegaScale | null | null | null | null | 1.025973 | null | null | null | null | null | null | -0.061055 | -1.292153 | 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":2364234,"numValue":-0.0610553763956368,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364235,"numValue":-1.292152560016917,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364236,"numValue":1.025973373410806,"references":[],"strValue":null,"t... | [{"id":20814,"numValue":9.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18081 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,081 | train | mutant | 475,838 | 358 | 477,210 | 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 | V6Q | V6Q | 1 | 1 | 0 | 0 | 6 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 6 | A | E | false | false | 1.970407 | 21.922857 | 5,064,337 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.779896 | 0.068596 | 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":12121356,"numValue":-0.779896335315332,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121357,"numValue":0.0685964774223219,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20814,"numValue":9.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18082 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,082 | train | mutant | 475,839 | 358 | 477,211 | 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 | V6E | V6E | 1 | 1 | 0 | 0 | 6 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 6 | A | E | false | false | 1.970407 | 21.922857 | 501,451 | MegaScale | null | null | null | null | -0.125608 | null | null | null | null | null | null | -0.357045 | -1.785538 | 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":2364237,"numValue":-0.3570448286924405,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364238,"numValue":-1.7855376947040669,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364239,"numValue":-0.1256078981885987,"references":[],"strValue":null... | [{"id":20814,"numValue":9.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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