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:19073 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,073 | train | mutant | 476,249 | 358 | 477,601 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25I | D25I | 1 | 1 | 0 | 0 | 25 | D | I | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,881 | MegaScale | null | null | null | null | 4.808947 | null | null | null | null | null | null | 2.040634 | 1.135099 | 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":2365527,"numValue":2.0406344990499914,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365528,"numValue":1.135099234243059,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365529,"numValue":4.808947129093681,"references":[],"strValue":null,"typ... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19074 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,074 | train | mutant | 476,249 | 358 | 477,601 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25I | D25I | 1 | 1 | 0 | 0 | 25 | D | I | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,340 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.874709 | 0.094294 | 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":12123362,"numValue":-0.874708727898634,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123363,"numValue":0.0942941120944402,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19075 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,075 | train | mutant | 476,250 | 358 | 477,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25W | D25W | 1 | 1 | 0 | 0 | 25 | D | W | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,882 | MegaScale | null | null | null | null | 4.964825 | null | null | null | null | null | null | 2.188819 | 1.205529 | 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":2365530,"numValue":2.188818660517041,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365531,"numValue":1.205528812074185,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365532,"numValue":4.964825324738788,"references":[],"strValue":null,"type... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19076 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,076 | train | mutant | 476,250 | 358 | 477,602 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25W | D25W | 1 | 1 | 0 | 0 | 25 | D | W | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,351 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.883515 | 0.073802 | 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":12123384,"numValue":-0.883514834751633,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123385,"numValue":0.0738018535795671,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19078 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,078 | train | mutant | 476,251 | 358 | 477,603 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Y | D25Y | 1 | 1 | 0 | 0 | 25 | D | Y | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,352 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.892454 | 0.079813 | 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":12123386,"numValue":-0.892453547807818,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123387,"numValue":0.0798126805509819,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19081 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,081 | train | mutant | 476,253 | 358 | 477,605 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25P | D25P | 1 | 1 | 0 | 0 | 25 | D | P | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,885 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.160445 | 1.54379 | 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":2365539,"numValue":2.160445034832656,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365540,"numValue":1.5437900496029595,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365541,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19082 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,082 | train | mutant | 476,253 | 358 | 477,605 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25P | D25P | 1 | 1 | 0 | 0 | 25 | D | P | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,345 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.168022 | 0.038659 | 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":12123372,"numValue":-0.168021627691463,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123373,"numValue":0.0386594678222338,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19083 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,083 | train | mutant | 476,254 | 358 | 477,606 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25C | D25C | 1 | 1 | 0 | 0 | 25 | D | C | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,886 | MegaScale | null | null | null | null | 4.649262 | null | null | null | null | null | null | 1.903654 | 1.050936 | 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":2365542,"numValue":1.9036540007471885,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365543,"numValue":1.0509362056311755,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365544,"numValue":4.649261621784733,"references":[],"strValue":null,"ty... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19084 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,084 | train | mutant | 476,254 | 358 | 477,606 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25C | D25C | 1 | 1 | 0 | 0 | 25 | D | C | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,064,496 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.386082 | 0.050816 | 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":12121674,"numValue":-0.386081549870881,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121675,"numValue":0.0508161506995284,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19085 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,085 | train | mutant | 476,255 | 358 | 477,607 | 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 | insG25 | insG25 | 1 | 0 | 0 | 1 | 25 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,887 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.888144 | 1.438438 | 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":2365545,"numValue":1.8881444518646304,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365546,"numValue":1.4384378307102716,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365547,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19086 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,086 | train | mutant | 476,256 | 358 | 477,608 | 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 | insA25 | insA25 | 1 | 0 | 0 | 1 | 25 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,888 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.858179 | 1.385715 | 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":2365548,"numValue":1.8581789842900636,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365549,"numValue":1.3857153752373668,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365550,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19087 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,087 | train | mutant | 476,257 | 358 | 477,609 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26Q | V26Q | 1 | 1 | 0 | 0 | 26 | V | Q | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,890 | MegaScale | null | null | null | null | 2.931509 | null | null | null | null | null | null | 1.047181 | 0.105754 | 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":2365554,"numValue":1.0471810842302505,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365555,"numValue":0.1057538332780215,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365556,"numValue":2.9315092488200856,"references":[],"strValue":null,"t... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19088 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,088 | train | mutant | 476,257 | 358 | 477,609 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26Q | V26Q | 1 | 1 | 0 | 0 | 26 | V | Q | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,511 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.514314 | 0.053569 | 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":12121704,"numValue":-0.514314017745311,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121705,"numValue":0.0535689254475291,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19089 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,089 | train | mutant | 476,258 | 358 | 477,610 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26E | V26E | 1 | 1 | 0 | 0 | 26 | V | E | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,891 | MegaScale | null | null | null | null | 1.009729 | null | null | null | null | null | null | -0.144012 | -1.295276 | 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":2365557,"numValue":-0.1440115756250951,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365558,"numValue":-1.2952760052734402,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365559,"numValue":1.0097293236271,"references":[],"strValue":null,"ty... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19090 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,090 | train | mutant | 476,258 | 358 | 477,610 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26E | V26E | 1 | 1 | 0 | 0 | 26 | V | E | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,501 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.717324 | 0.056475 | 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":12121684,"numValue":-0.717324362562533,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121685,"numValue":0.0564754056280845,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19091 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,091 | train | mutant | 476,259 | 358 | 477,611 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26N | V26N | 1 | 1 | 0 | 0 | 26 | V | N | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,892 | MegaScale | null | null | null | null | 1.836785 | null | null | null | null | null | null | 0.447935 | -0.735913 | 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":2365560,"numValue":0.4479345861653164,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365561,"numValue":-0.735913369515897,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365562,"numValue":1.836784788488174,"references":[],"strValue":null,"ty... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19092 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,092 | train | mutant | 476,259 | 358 | 477,611 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26N | V26N | 1 | 1 | 0 | 0 | 26 | V | N | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,509 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.617093 | 0.090614 | 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":12121700,"numValue":-0.61709259611481,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121701,"numValue":0.0906144432934597,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19093 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,093 | train | mutant | 476,260 | 358 | 477,612 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26H | V26H | 1 | 1 | 0 | 0 | 26 | V | H | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,893 | MegaScale | null | null | null | null | 3.199682 | null | null | null | null | null | null | 1.264749 | 0.196046 | 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":2365563,"numValue":1.2647487318770845,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365564,"numValue":0.1960457796256662,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365565,"numValue":3.1996817107397897,"references":[],"strValue":null,"t... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19094 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,094 | train | mutant | 476,260 | 358 | 477,612 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26H | V26H | 1 | 1 | 0 | 0 | 26 | V | H | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,504 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.580958 | 0.0879 | 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":12121690,"numValue":-0.580958264436274,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121691,"numValue":0.087900002901144,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19095 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,095 | train | mutant | 476,261 | 358 | 477,613 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26D | V26D | 1 | 1 | 0 | 0 | 26 | V | D | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,894 | MegaScale | null | null | null | null | 0.055539 | null | null | null | null | null | null | -0.610959 | -1.781647 | 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":2365566,"numValue":-0.6109585995216342,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365567,"numValue":-1.78164743712076,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365568,"numValue":0.0555392132125978,"references":[],"strValue":null,"t... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19096 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,096 | train | mutant | 476,261 | 358 | 477,613 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26D | V26D | 1 | 1 | 0 | 0 | 26 | V | D | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,500 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.749545 | 0.14634 | 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":12121682,"numValue":-0.749545277872864,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121683,"numValue":0.146339593446064,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19097 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,097 | train | mutant | 476,262 | 358 | 477,614 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26R | V26R | 1 | 1 | 0 | 0 | 26 | V | R | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,895 | MegaScale | null | null | null | null | 3.286137 | null | null | null | null | null | null | 1.348947 | 0.315539 | 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":2365569,"numValue":1.3489467163118958,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365570,"numValue":0.3155385855925446,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365571,"numValue":3.286136618737368,"references":[],"strValue":null,"ty... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19098 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,098 | train | mutant | 476,262 | 358 | 477,614 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26R | V26R | 1 | 1 | 0 | 0 | 26 | V | R | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,512 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.655376 | 0.033708 | 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":12121706,"numValue":-0.655376411785318,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121707,"numValue":0.0337077792306669,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19099 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,099 | train | mutant | 476,263 | 358 | 477,615 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26K | V26K | 1 | 1 | 0 | 0 | 26 | V | K | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,896 | MegaScale | null | null | null | null | 3.60485 | null | null | null | null | null | null | 1.469142 | 0.546495 | 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":2365572,"numValue":1.4691415010570148,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365573,"numValue":0.5464953693648427,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365574,"numValue":3.6048495133292175,"references":[],"strValue":null,"t... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19100 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,100 | train | mutant | 476,263 | 358 | 477,615 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26K | V26K | 1 | 1 | 0 | 0 | 26 | V | K | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,506 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.372786 | 0.046998 | 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":12121694,"numValue":-0.372785968619926,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121695,"numValue":0.0469984659510879,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19101 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,101 | train | mutant | 476,264 | 358 | 477,616 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26T | V26T | 1 | 1 | 0 | 0 | 26 | V | T | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,897 | MegaScale | null | null | null | null | 4.991321 | null | null | null | null | null | null | 2.131964 | 1.371189 | 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":2365575,"numValue":2.1319643792688634,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365576,"numValue":1.3711888487371375,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365577,"numValue":4.991321493955013,"references":[],"strValue":null,"ty... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19102 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,102 | train | mutant | 476,264 | 358 | 477,616 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26T | V26T | 1 | 1 | 0 | 0 | 26 | V | T | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,514 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.159461 | 0.042348 | 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":12121710,"numValue":-0.159461106054724,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121711,"numValue":0.0423478523223229,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19103 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,103 | train | mutant | 476,265 | 358 | 477,617 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26S | V26S | 1 | 1 | 0 | 0 | 26 | V | S | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,898 | MegaScale | null | null | null | null | 3.40934 | null | null | null | null | null | null | 1.38569 | 0.481795 | 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":2365578,"numValue":1.3856896142445012,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365579,"numValue":0.4817946865656449,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365580,"numValue":3.4093397223713966,"references":[],"strValue":null,"t... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19104 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,104 | train | mutant | 476,265 | 358 | 477,617 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26S | V26S | 1 | 1 | 0 | 0 | 26 | V | S | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,513 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.494786 | 0.037926 | 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":12121708,"numValue":-0.49478582227469,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121709,"numValue":0.0379261959996965,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19105 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,105 | train | mutant | 476,266 | 358 | 477,618 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26A | V26A | 1 | 1 | 0 | 0 | 26 | V | A | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,899 | MegaScale | null | null | null | null | 4.08693 | null | null | null | null | null | null | 1.962624 | 0.78345 | 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":2365581,"numValue":1.9626236833473445,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365582,"numValue":0.7834497013020623,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365583,"numValue":4.086929987211908,"references":[],"strValue":null,"ty... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19106 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,106 | train | mutant | 476,266 | 358 | 477,618 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26A | V26A | 1 | 1 | 0 | 0 | 26 | V | A | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,498 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.314588 | 0.040271 | 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":12121678,"numValue":-0.31458828319312,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121679,"numValue":0.0402714366790353,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19107 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,107 | train | mutant | 476,267 | 358 | 477,619 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26G | V26G | 1 | 1 | 0 | 0 | 26 | V | G | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,900 | MegaScale | null | null | null | null | 0.593446 | null | null | null | null | null | null | -0.269425 | -1.58994 | 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":2365584,"numValue":-0.2694253297102452,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365585,"numValue":-1.5899401227689527,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365586,"numValue":0.593445625010838,"references":[],"strValue":null,"... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19109 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,109 | train | mutant | 476,268 | 358 | 477,620 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26M | V26M | 1 | 1 | 0 | 0 | 26 | V | M | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,901 | MegaScale | null | null | null | null | 4.712837 | null | null | null | null | null | null | 2.082218 | 1.204225 | 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":2365587,"numValue":2.082217547958912,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365588,"numValue":1.2042245995259604,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365589,"numValue":4.712836703664506,"references":[],"strValue":null,"typ... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19110 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,110 | train | mutant | 476,268 | 358 | 477,620 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26M | V26M | 1 | 1 | 0 | 0 | 26 | V | M | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,508 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.183566 | 0.041257 | 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":12121698,"numValue":-0.18356574890948,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121699,"numValue":0.041257095765906,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19111 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,111 | train | mutant | 476,269 | 358 | 477,621 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26L | V26L | 1 | 1 | 0 | 0 | 26 | V | L | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,902 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.6068 | 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":2365590,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365591,"numValue":1.6068001183417342,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365592,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19113 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,113 | train | mutant | 476,270 | 358 | 477,622 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26I | V26I | 1 | 1 | 0 | 0 | 26 | V | I | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,903 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.646169 | 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":2365593,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365594,"numValue":1.646168903833878,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365595,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19114 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,114 | train | mutant | 476,270 | 358 | 477,622 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26I | V26I | 1 | 1 | 0 | 0 | 26 | V | I | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,505 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.038486 | 0.050458 | 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":12121692,"numValue":-0.0384864664084015,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121693,"numValue":0.050458451293257,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19115 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,115 | train | mutant | 476,271 | 358 | 477,623 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26W | V26W | 1 | 1 | 0 | 0 | 26 | V | W | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,904 | MegaScale | null | null | null | null | 3.773309 | null | null | null | null | null | null | 1.78719 | 0.65523 | 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":2365596,"numValue":1.7871895194364475,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365597,"numValue":0.65523042915518,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365598,"numValue":3.773308700280455,"references":[],"strValue":null,"type... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19116 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,116 | train | mutant | 476,271 | 358 | 477,623 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26W | V26W | 1 | 1 | 0 | 0 | 26 | V | W | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,065,334 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.696497 | 0.045408 | 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":12123350,"numValue":-0.696496724436643,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123351,"numValue":0.0454079152654949,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19118 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,118 | train | mutant | 476,272 | 358 | 477,624 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26Y | V26Y | 1 | 1 | 0 | 0 | 26 | V | Y | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,065,335 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.320381 | 0.075605 | 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":12123352,"numValue":-0.320380757674553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123353,"numValue":0.0756051016709915,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19119 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,119 | train | mutant | 476,273 | 358 | 477,625 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26F | V26F | 1 | 1 | 0 | 0 | 26 | V | F | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,906 | MegaScale | null | null | null | null | 4.706868 | null | null | null | null | null | null | 2.080196 | 1.236014 | 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":2365602,"numValue":2.0801961093075287,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365603,"numValue":1.2360141978700685,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365604,"numValue":4.7068678228765695,"references":[],"strValue":null,"t... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19120 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,120 | train | mutant | 476,273 | 358 | 477,625 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26F | V26F | 1 | 1 | 0 | 0 | 26 | V | F | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,502 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.288155 | 0.050528 | 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":12121686,"numValue":-0.288154751561788,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121687,"numValue":0.0505278395437954,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19122 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,122 | train | mutant | 476,274 | 358 | 477,626 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26P | V26P | 1 | 1 | 0 | 0 | 26 | V | P | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,510 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.75914 | 0.067507 | 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":12121702,"numValue":-0.759140213763408,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121703,"numValue":0.067507352376083,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19123 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,123 | train | mutant | 476,275 | 358 | 477,627 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26C | V26C | 1 | 1 | 0 | 0 | 26 | V | C | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,908 | MegaScale | null | null | null | null | 4.546354 | null | null | null | null | null | null | 1.998555 | 1.042353 | 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":2365608,"numValue":1.998554786921554,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365609,"numValue":1.0423527226357487,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365610,"numValue":4.546353876404636,"references":[],"strValue":null,"typ... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19124 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,124 | train | mutant | 476,275 | 358 | 477,627 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V26C | V26C | 1 | 1 | 0 | 0 | 26 | V | C | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,499 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.090706 | 0.075764 | 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":12121680,"numValue":-0.0907064457471037,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121681,"numValue":0.0757644499207031,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,127 | train | mutant | 476,278 | 358 | 477,630 | 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 | delV26 | delV26 | 1 | 0 | 1 | 0 | 26 | V | - | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 501,911 | MegaScale | null | null | null | null | 0.100215 | null | null | null | null | null | null | -0.677854 | -1.752414 | 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":2365617,"numValue":-0.6778536453707521,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365618,"numValue":-1.7524143576658688,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365619,"numValue":0.100214868447283,"references":[],"strValue":null,"... | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,128 | train | mutant | 476,278 | 358 | 477,630 | 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 | delV26 | delV26 | 1 | 0 | 1 | 0 | 26 | V | - | 6 | CONSERVATION | 1CSP | 247 | null | 26 | A | E | false | false | 7.927886 | 27.778571 | 5,064,497 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.105996 | 0.084586 | 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":12121676,"numValue":-1.10599586123896,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121677,"numValue":0.0845861971908216,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20834,"numValue":6.0,"position":26,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,129 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 3,369 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | null | 1CSP_A:F27A | 53.9 | -6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:F27A",... | [{"datasets":[],"id":12421,"numValue":53.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12422,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12423,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,130 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 7,105 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | 60 | 1CSP_A:F27A | null | null | null | 0.69 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type... | [{"datasets":["capriotti_S1615_map.csv","SAAFEC_S983.csv"],"id":24931,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24932,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19131 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,131 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 7,872 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F27A | null | null | 0.28 | 0.89 | null | 0.91 | 33.46 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":26907,"numValue":0.91,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26908,"numValue":33.46,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26909,"numValue":0.28,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":26910,"numValue":0.89,"references"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:19132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,132 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 7,873 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F27A | null | null | 14.36 | 0.12 | null | -1 | -4.04 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":26912,"numValue":-1.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26913,"numValue":-4.04,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26914,"numValue":14.36,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":26... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19133 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,133 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 7,876 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F27A | null | null | 14.51 | 0.88 | null | -0.12 | 29.4 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":26927,"numValue":-0.12,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26928,"numValue":29.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26929,"numValue":14.51,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":26930,"numValue":0.88,"references... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:19134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,134 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 10,699 | ProTherm | 7 | CD | Urea | Potassium phosphate | 0.35 M | 25 | 1CSP_A:F27A | null | null | 2.73 | 0.76 | null | null | null | 3.17 | 0.86 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"... | [{"datasets":[],"id":36732,"numValue":2.73,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":36733,"numValue":0.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36734,"numValue":0.86,"references":[],"strValue":... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19135 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,135 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,921 | MegaScale | null | null | null | null | 3.18445 | null | null | null | null | null | null | 1.446251 | 0.27398 | 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":2365647,"numValue":1.4462505236494183,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365648,"numValue":0.2739798101506474,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365649,"numValue":3.184450083958498,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19136 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,136 | train | mutant | 1,766 | 358 | 1,979 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27A | F27A | 1 | 1 | 0 | 0 | 27 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,064,516 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.243697 | 0.035412 | 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":12121714,"numValue":-0.243697325911884,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121715,"numValue":0.0354124497597601,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19137 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,137 | train | mutant | 476,279 | 358 | 477,631 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27Q | F27Q | 1 | 1 | 0 | 0 | 27 | F | Q | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,912 | MegaScale | null | null | null | null | 2.7639 | null | null | null | null | null | null | 1.116029 | -0.062054 | 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":2365620,"numValue":1.1160291081533062,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365621,"numValue":-0.0620539515738525,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365622,"numValue":2.7638995864000284,"references":[],"strValue":null,"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,138 | train | mutant | 476,279 | 358 | 477,631 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27Q | F27Q | 1 | 1 | 0 | 0 | 27 | F | Q | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,327 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.274767 | 0.041263 | 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":12123336,"numValue":-0.274766554507498,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123337,"numValue":0.0412626159131247,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19139 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,139 | train | mutant | 476,280 | 358 | 477,632 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27E | F27E | 1 | 1 | 0 | 0 | 27 | F | E | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,913 | MegaScale | null | null | null | null | 2.204278 | null | null | null | null | null | null | 0.556762 | -0.149201 | 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":2365623,"numValue":0.5567616770314568,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365624,"numValue":-0.1492014248347699,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365625,"numValue":2.2042779975320315,"references":[],"strValue":null,"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,140 | train | mutant | 476,280 | 358 | 477,632 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27E | F27E | 1 | 1 | 0 | 0 | 27 | F | E | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,064,519 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.178017 | 0.050604 | 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":12121720,"numValue":-0.178017387605049,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121721,"numValue":0.0506040237089096,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19141 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,141 | train | mutant | 476,281 | 358 | 477,633 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27N | F27N | 1 | 1 | 0 | 0 | 27 | F | N | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,914 | MegaScale | null | null | null | null | 2.624254 | null | null | null | null | null | null | 0.910591 | 0.010516 | 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":2365626,"numValue":0.9105914853139584,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365627,"numValue":0.0105160891299154,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365628,"numValue":2.624253799459704,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,142 | train | mutant | 476,281 | 358 | 477,633 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27N | F27N | 1 | 1 | 0 | 0 | 27 | F | N | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,325 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.710382 | 0.114377 | 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":12123332,"numValue":-0.710381612070673,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123333,"numValue":0.114377021025566,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19143 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,143 | train | mutant | 476,282 | 358 | 477,634 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27H | F27H | 1 | 1 | 0 | 0 | 27 | F | H | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,915 | MegaScale | null | null | null | null | 3.142907 | null | null | null | null | null | null | 1.428027 | 0.323315 | 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":2365629,"numValue":1.4280273641272836,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365630,"numValue":0.3233148651189678,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365631,"numValue":3.1429073506961585,"references":[],"strValue":null,"t... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,145 | train | mutant | 476,283 | 358 | 477,635 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27D | F27D | 1 | 1 | 0 | 0 | 27 | F | D | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,916 | MegaScale | null | null | null | null | 0.466602 | null | null | null | null | null | null | -0.42304 | -1.25974 | 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":2365632,"numValue":-0.423040375113124,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365633,"numValue":-1.2597398783863016,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365634,"numValue":0.4666016280701212,"references":[],"strValue":null,"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19146 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,146 | train | mutant | 476,283 | 358 | 477,635 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27D | F27D | 1 | 1 | 0 | 0 | 27 | F | D | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,064,518 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.634411 | 0.095226 | 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":12121718,"numValue":-0.634410524639085,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121719,"numValue":0.0952264649596695,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19147 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,147 | train | mutant | 476,284 | 358 | 477,636 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27R | F27R | 1 | 1 | 0 | 0 | 27 | F | R | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,917 | MegaScale | null | null | null | null | 3.277907 | null | null | null | null | null | null | 1.310717 | 0.236551 | 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":2365635,"numValue":1.3107165039862747,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365636,"numValue":0.2365513851015669,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365637,"numValue":3.277907202427242,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19148 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,148 | train | mutant | 476,284 | 358 | 477,636 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27R | F27R | 1 | 1 | 0 | 0 | 27 | F | R | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,328 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.224066 | 0.03331 | 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":12123338,"numValue":-0.224066455702996,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123339,"numValue":0.0333102120944831,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19150 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,150 | train | mutant | 476,285 | 358 | 477,637 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27K | F27K | 1 | 1 | 0 | 0 | 27 | F | K | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,322 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.304336 | 0.040857 | 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":12123326,"numValue":-0.304336143108713,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123327,"numValue":0.0408570629639645,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,151 | train | mutant | 476,286 | 358 | 477,638 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27T | F27T | 1 | 1 | 0 | 0 | 27 | F | T | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,919 | MegaScale | null | null | null | null | 1.923744 | null | null | null | null | null | null | 0.48214 | -0.601261 | 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":2365641,"numValue":0.4821403058567231,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365642,"numValue":-0.6012613251023696,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365643,"numValue":1.9237436117449624,"references":[],"strValue":null,"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19152 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,152 | train | mutant | 476,286 | 358 | 477,638 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27T | F27T | 1 | 1 | 0 | 0 | 27 | F | T | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,330 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.471594 | 0.047205 | 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":12123342,"numValue":-0.471593782425115,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123343,"numValue":0.0472046434497044,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19153 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,153 | train | mutant | 476,287 | 358 | 477,639 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27S | F27S | 1 | 1 | 0 | 0 | 27 | F | S | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,920 | MegaScale | null | null | null | null | 2.688876 | null | null | null | null | null | null | 0.989124 | -0.059221 | 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":2365644,"numValue":0.9891243029772478,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365645,"numValue":-0.0592210402914487,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365646,"numValue":2.6888757199119757,"references":[],"strValue":null,"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,154 | train | mutant | 476,287 | 358 | 477,639 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27S | F27S | 1 | 1 | 0 | 0 | 27 | F | S | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,329 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.332661 | 0.037061 | 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":12123340,"numValue":-0.332660631837277,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123341,"numValue":0.0370610785275903,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19155 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,155 | train | mutant | 476,288 | 358 | 477,640 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27G | F27G | 1 | 1 | 0 | 0 | 27 | F | G | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,922 | MegaScale | null | null | null | null | 1.846772 | null | null | null | null | null | null | 0.536285 | -0.711843 | 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":2365650,"numValue":0.5362845624239514,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365651,"numValue":-0.711842549634143,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365652,"numValue":1.846771635760829,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,156 | train | mutant | 476,288 | 358 | 477,640 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27G | F27G | 1 | 1 | 0 | 0 | 27 | F | G | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,319 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.424632 | 0.037662 | 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":12123320,"numValue":-0.424631804647142,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123321,"numValue":0.0376624249650989,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,157 | train | mutant | 476,289 | 358 | 477,641 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27M | F27M | 1 | 1 | 0 | 0 | 27 | F | M | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,923 | MegaScale | null | null | null | null | 3.736671 | null | null | null | null | null | null | 1.724287 | 0.600391 | 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":2365653,"numValue":1.7242865467021844,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365654,"numValue":0.6003913542677406,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365655,"numValue":3.736671280757329,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19158 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,158 | train | mutant | 476,289 | 358 | 477,641 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27M | F27M | 1 | 1 | 0 | 0 | 27 | F | M | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,324 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.244235 | 0.038729 | 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":12123330,"numValue":-0.244235233590856,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123331,"numValue":0.0387285187304422,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19159 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,159 | train | mutant | 476,290 | 358 | 477,642 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27L | F27L | 1 | 1 | 0 | 0 | 27 | F | L | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,924 | MegaScale | null | null | null | null | 4.144187 | null | null | null | null | null | null | 1.803642 | 0.974242 | 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":2365656,"numValue":1.803641669728476,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365657,"numValue":0.9742416967434472,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365658,"numValue":4.1441866306662,"references":[],"strValue":null,"type"... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,160 | train | mutant | 476,290 | 358 | 477,642 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27L | F27L | 1 | 1 | 0 | 0 | 27 | F | L | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,323 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.245832 | 0.030484 | 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":12123328,"numValue":-0.245831782836427,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123329,"numValue":0.0304836575121567,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,161 | train | mutant | 476,291 | 358 | 477,643 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27V | F27V | 1 | 1 | 0 | 0 | 27 | F | V | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,925 | MegaScale | null | null | null | null | 3.024332 | null | null | null | null | null | null | 1.203839 | 0.223677 | 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":2365659,"numValue":1.2038394167652156,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365660,"numValue":0.2236774866168971,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365661,"numValue":3.0243316747954188,"references":[],"strValue":null,"t... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19162 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,162 | train | mutant | 476,291 | 358 | 477,643 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27V | F27V | 1 | 1 | 0 | 0 | 27 | F | V | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,331 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.307248 | 0.031401 | 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":12123344,"numValue":-0.307247714091703,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123345,"numValue":0.0314005232976893,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,163 | train | mutant | 476,292 | 358 | 477,644 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27I | F27I | 1 | 1 | 0 | 0 | 27 | F | I | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,926 | MegaScale | null | null | null | null | 3.305475 | null | null | null | null | null | null | 1.440656 | 0.275848 | 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":2365662,"numValue":1.4406564663460109,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365663,"numValue":0.275848282284942,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365664,"numValue":3.3054745287046927,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19164 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,164 | train | mutant | 476,292 | 358 | 477,644 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27I | F27I | 1 | 1 | 0 | 0 | 27 | F | I | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,321 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.275181 | 0.052597 | 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":12123324,"numValue":-0.275181178898587,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123325,"numValue":0.0525966189834306,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19165 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,165 | train | mutant | 476,293 | 358 | 477,645 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27W | F27W | 1 | 1 | 0 | 0 | 27 | F | W | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,927 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.206773 | 1.362474 | 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":2365665,"numValue":2.206772666026905,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365666,"numValue":1.362474208634584,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365667,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,166 | train | mutant | 476,293 | 358 | 477,645 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27W | F27W | 1 | 1 | 0 | 0 | 27 | F | W | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,332 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.120488 | 0.04163 | 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":12123346,"numValue":-0.120488253341391,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123347,"numValue":0.0416297977056183,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19167 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,167 | train | mutant | 476,294 | 358 | 477,646 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27Y | F27Y | 1 | 1 | 0 | 0 | 27 | F | Y | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,928 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.162418 | 1.450821 | 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":2365668,"numValue":2.162418390159262,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365669,"numValue":1.4508205401316636,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365670,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19168 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,168 | train | mutant | 476,294 | 358 | 477,646 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27Y | F27Y | 1 | 1 | 0 | 0 | 27 | F | Y | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,333 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.077645 | 0.054476 | 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":12123348,"numValue":-0.0776445507284048,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123349,"numValue":0.05447640698279,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,169 | train | mutant | 476,295 | 358 | 477,647 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27P | F27P | 1 | 1 | 0 | 0 | 27 | F | P | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,929 | MegaScale | null | null | null | null | 3.523824 | null | null | null | null | null | null | 1.582058 | 0.548436 | 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":2365671,"numValue":1.582057550197091,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365672,"numValue":0.5484364147371008,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365673,"numValue":3.5238238621829057,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19170 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,170 | train | mutant | 476,295 | 358 | 477,647 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27P | F27P | 1 | 1 | 0 | 0 | 27 | F | P | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,065,326 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.156986 | 0.040861 | 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":12123334,"numValue":-0.156985626702007,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123335,"numValue":0.0408608534650547,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,171 | train | mutant | 476,296 | 358 | 477,648 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F27C | F27C | 1 | 1 | 0 | 0 | 27 | F | C | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,930 | MegaScale | null | null | null | null | 2.843773 | null | null | null | null | null | null | 0.971281 | 0.045311 | 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":2365674,"numValue":0.971280904222012,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365675,"numValue":0.0453110644507165,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365676,"numValue":2.8437728343311663,"references":[],"strValue":null,"ty... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19173 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,173 | train | mutant | 476,297 | 358 | 477,649 | 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 | insG27 | insG27 | 1 | 0 | 0 | 1 | 27 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,931 | MegaScale | null | null | null | null | 0.276161 | null | null | null | null | null | null | -0.618133 | -1.715529 | 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":2365677,"numValue":-0.6181325691507122,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365678,"numValue":-1.7155286245143264,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365679,"numValue":0.2761613435456259,"references":[],"strValue":null,... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19175 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,175 | train | mutant | 476,299 | 358 | 477,651 | 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 | delF27 | delF27 | 1 | 0 | 1 | 0 | 27 | F | - | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 501,933 | MegaScale | null | null | null | null | -0.008425 | null | null | null | null | null | null | -0.641022 | -1.777957 | 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":2365683,"numValue":-0.6410219031504576,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365684,"numValue":-1.7779570898065984,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365685,"numValue":-0.0084250829575811,"references":[],"strValue":null... | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19176 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,176 | train | mutant | 476,299 | 358 | 477,651 | 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 | delF27 | delF27 | 1 | 0 | 1 | 0 | 27 | F | - | 9 | CONSERVATION | 1CSP | 247 | null | 27 | A | E | true | false | 72.045413 | 12.702727 | 5,064,515 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.147747 | 0.112126 | 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":12121712,"numValue":-1.14774698564694,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121713,"numValue":0.112126211664648,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19177 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,177 | train | mutant | 476,300 | 358 | 477,652 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q | V28Q | 1 | 1 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,934 | MegaScale | null | null | null | null | 0.484746 | null | null | null | null | null | null | -0.521391 | -1.607544 | 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":2365686,"numValue":-0.5213910961836665,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365687,"numValue":-1.6075440198726243,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365688,"numValue":0.4847459723032659,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19178 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,178 | train | mutant | 476,300 | 358 | 477,652 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q | V28Q | 1 | 1 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,501 | MegaScale | null | null | null | null | 0.510701 | null | null | null | null | null | null | -0.408245 | -1.591002 | 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":3525897,"numValue":-0.4082446779700183,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525898,"numValue":-1.591002468331882,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525899,"numValue":0.5107007842361381,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19179 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,179 | train | mutant | 476,300 | 358 | 477,652 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q | V28Q | 1 | 1 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,534 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.729458 | 0.071322 | 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":12121750,"numValue":-0.729458075493901,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121751,"numValue":0.0713221421139821,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19180 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,180 | train | mutant | 476,301 | 358 | 477,653 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E | V28E | 1 | 1 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,935 | MegaScale | null | null | null | null | 0.284731 | null | null | null | null | null | null | -0.583727 | -1.502923 | 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":2365689,"numValue":-0.5837270368081853,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365690,"numValue":-1.502922501409363,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365691,"numValue":0.2847310526883846,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19181 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,181 | train | mutant | 476,301 | 358 | 477,653 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E | V28E | 1 | 1 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,521 | MegaScale | null | null | null | null | 0.346459 | null | null | null | null | null | null | -0.633102 | -1.439331 | 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":3525957,"numValue":-0.6331020169039834,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525958,"numValue":-1.4393310875500678,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525959,"numValue":0.3464589586371674,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19182 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,182 | train | mutant | 476,301 | 358 | 477,653 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E | V28E | 1 | 1 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,524 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.672881 | 0.049764 | 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":12121730,"numValue":-0.672881350630367,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121731,"numValue":0.0497635506273862,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19183 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,183 | train | mutant | 476,302 | 358 | 477,654 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28N | V28N | 1 | 1 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,936 | MegaScale | null | null | null | null | 0.362221 | null | null | null | null | null | null | -0.472947 | -1.598297 | 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":2365692,"numValue":-0.4729469159393209,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365693,"numValue":-1.5982973852426992,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365694,"numValue":0.3622212740543036,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19185 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,185 | train | mutant | 476,302 | 358 | 477,654 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28N | V28N | 1 | 1 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,532 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.541094 | 0.188862 | 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":12121746,"numValue":-0.541094337291913,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121747,"numValue":0.188862146160863,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19187 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,187 | train | mutant | 476,303 | 358 | 477,655 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H | V28H | 1 | 1 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,561 | MegaScale | null | null | null | null | 0.638072 | null | null | null | null | null | null | -0.459862 | -1.432872 | 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":3526077,"numValue":-0.4598620838775753,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526078,"numValue":-1.4328723509675276,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526079,"numValue":0.6380717257032473,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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