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:18525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,525 | train | mutant | 476,039 | 358 | 477,391 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15S | F15S | 1 | 1 | 0 | 0 | 15 | F | S | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,656 | MegaScale | null | null | null | null | 3.856358 | null | null | null | null | null | null | 1.8619 | 0.671681 | 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":2364852,"numValue":1.8619004998712023,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364853,"numValue":0.6716808290410811,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364854,"numValue":3.8563581007281726,"references":[],"strValue":null,"t... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,526 | train | mutant | 476,039 | 358 | 477,391 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15S | F15S | 1 | 1 | 0 | 0 | 15 | F | S | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,475 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.299637 | 0.031282 | 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":12123632,"numValue":-0.299636657776572,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123633,"numValue":0.0312816315935935,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,527 | train | mutant | 476,040 | 358 | 477,392 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15G | F15G | 1 | 1 | 0 | 0 | 15 | F | G | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,658 | MegaScale | null | null | null | null | 2.367966 | null | null | null | null | null | null | 0.778728 | -0.325154 | 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":2364858,"numValue":0.7787276417350393,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364859,"numValue":-0.325153603824846,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364860,"numValue":2.3679664280153623,"references":[],"strValue":null,"t... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,528 | train | mutant | 476,040 | 358 | 477,392 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15G | F15G | 1 | 1 | 0 | 0 | 15 | F | G | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,465 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.565245 | 0.043068 | 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":12123612,"numValue":-0.565245226713366,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123613,"numValue":0.0430676120511683,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,529 | train | mutant | 476,041 | 358 | 477,393 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15M | F15M | 1 | 1 | 0 | 0 | 15 | F | M | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,659 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.620839 | 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":2364861,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364862,"numValue":1.6208394447120713,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364863,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,530 | train | mutant | 476,041 | 358 | 477,393 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15M | F15M | 1 | 1 | 0 | 0 | 15 | F | M | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,470 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.123887 | 0.044695 | 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":12123622,"numValue":-0.123887437328695,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123623,"numValue":0.0446947245118396,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,531 | train | mutant | 476,042 | 358 | 477,394 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15L | F15L | 1 | 1 | 0 | 0 | 15 | F | L | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,660 | MegaScale | null | null | null | null | 4.94232 | null | null | null | null | null | null | 2.122892 | 1.362202 | 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":2364864,"numValue":2.122892096666779,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364865,"numValue":1.3622021769170072,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364866,"numValue":4.942319934948706,"references":[],"strValue":null,"typ... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,532 | train | mutant | 476,042 | 358 | 477,394 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15L | F15L | 1 | 1 | 0 | 0 | 15 | F | L | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,469 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.246736 | 0.028923 | 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":12123620,"numValue":-0.246735860280903,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123621,"numValue":0.0289230812259609,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,533 | train | mutant | 476,043 | 358 | 477,395 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15V | F15V | 1 | 1 | 0 | 0 | 15 | F | V | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,661 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.14467 | 1.484776 | 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":2364867,"numValue":2.1446702589049926,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364868,"numValue":1.4847756934045195,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364869,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,534 | train | mutant | 476,043 | 358 | 477,395 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15V | F15V | 1 | 1 | 0 | 0 | 15 | F | V | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,477 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.134408 | 0.036264 | 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":12123636,"numValue":-0.134408224577744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123637,"numValue":0.0362638220652919,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,535 | train | mutant | 476,044 | 358 | 477,396 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15I | F15I | 1 | 1 | 0 | 0 | 15 | F | I | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,662 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.135497 | 1.522574 | 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":2364870,"numValue":2.135496671019353,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364871,"numValue":1.5225740006027513,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364872,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,536 | train | mutant | 476,044 | 358 | 477,396 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15I | F15I | 1 | 1 | 0 | 0 | 15 | F | I | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,467 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.077899 | 0.066888 | 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":12123616,"numValue":-0.0778990908501535,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123617,"numValue":0.0668882985329964,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,537 | train | mutant | 476,045 | 358 | 477,397 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15W | F15W | 1 | 1 | 0 | 0 | 15 | F | W | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,663 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364873,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364874,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364875,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,538 | train | mutant | 476,045 | 358 | 477,397 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15W | F15W | 1 | 1 | 0 | 0 | 15 | F | W | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,478 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.021013 | 0.048583 | 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":12123638,"numValue":0.0210127470626224,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123639,"numValue":0.048583453554984,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,539 | train | mutant | 476,046 | 358 | 477,398 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15Y | F15Y | 1 | 1 | 0 | 0 | 15 | F | Y | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,664 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364876,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364877,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364878,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,540 | train | mutant | 476,046 | 358 | 477,398 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15Y | F15Y | 1 | 1 | 0 | 0 | 15 | F | Y | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,479 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.005653 | 0.088102 | 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":12123640,"numValue":0.00565324410158468,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123641,"numValue":0.0881015496095937,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18541 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,541 | train | mutant | 476,047 | 358 | 477,399 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15P | F15P | 1 | 1 | 0 | 0 | 15 | F | P | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,665 | MegaScale | null | null | null | null | -0.28818 | null | null | null | null | null | null | -0.73889 | -1.843908 | 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":2364879,"numValue":-0.7388899084740761,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364880,"numValue":-1.8439079636900824,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364881,"numValue":-0.2881801832461538,"references":[],"strValue":null... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,542 | train | mutant | 476,047 | 358 | 477,399 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15P | F15P | 1 | 1 | 0 | 0 | 15 | F | P | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,472 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.725122 | 0.047636 | 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":12123626,"numValue":-0.725121509173902,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123627,"numValue":0.0476360490883385,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,543 | train | mutant | 476,048 | 358 | 477,400 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15C | F15C | 1 | 1 | 0 | 0 | 15 | F | C | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,666 | MegaScale | null | null | null | null | 4.31598 | null | null | null | null | null | null | 1.865509 | 0.955802 | 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":2364882,"numValue":1.8655086613753973,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364883,"numValue":0.9558015732953774,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364884,"numValue":4.315979724643574,"references":[],"strValue":null,"ty... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,544 | train | mutant | 476,048 | 358 | 477,400 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15C | F15C | 1 | 1 | 0 | 0 | 15 | F | C | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,064,423 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.174569 | 0.054587 | 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":12121528,"numValue":-0.174569135642468,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121529,"numValue":0.0545873128739095,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18545 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,545 | train | mutant | 476,049 | 358 | 477,401 | 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 | insA15 | insA15 | 1 | 0 | 0 | 1 | 15 | - | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,668 | MegaScale | null | null | null | null | 2.880816 | null | null | null | null | null | null | 0.894823 | -0.024823 | 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":2364888,"numValue":0.8948231279942638,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364889,"numValue":-0.0248234063583307,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364890,"numValue":2.880815876034834,"references":[],"strValue":null,"t... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,547 | train | mutant | 476,050 | 358 | 477,402 | 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 | delF15 | delF15 | 1 | 0 | 1 | 0 | 15 | F | - | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,064,421 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.009804 | 0.095824 | 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":12121524,"numValue":-1.0098042108051,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121525,"numValue":0.0958241128985416,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18548 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,548 | train | mutant | 476,051 | 358 | 477,403 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16Q | G16Q | 1 | 1 | 0 | 0 | 16 | G | Q | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,670 | MegaScale | null | null | null | null | -0.039309 | null | null | null | null | null | null | -0.609425 | -1.85979 | 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":2364894,"numValue":-0.6094253133459088,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364895,"numValue":-1.8597899649334104,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364896,"numValue":-0.0393089785380598,"references":[],"strValue":null... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,549 | train | mutant | 476,051 | 358 | 477,403 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16Q | G16Q | 1 | 1 | 0 | 0 | 16 | G | Q | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,458 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.684536 | 0.064836 | 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":12123598,"numValue":-0.684536466797878,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123599,"numValue":0.0648363984768564,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,550 | train | mutant | 476,052 | 358 | 477,404 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16E | G16E | 1 | 1 | 0 | 0 | 16 | G | E | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,671 | MegaScale | null | null | null | null | -0.441178 | null | null | null | null | null | null | -0.69773 | -1.713928 | 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":2364897,"numValue":-0.6977300020826374,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364898,"numValue":-1.71392766419606,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364899,"numValue":-0.4411775706370887,"references":[],"strValue":null,"... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,551 | train | mutant | 476,052 | 358 | 477,404 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16E | G16E | 1 | 1 | 0 | 0 | 16 | G | E | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,064,430 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.871089 | 0.072267 | 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":12121542,"numValue":-0.871089474042213,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121543,"numValue":0.072267007312907,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,552 | train | mutant | 476,053 | 358 | 477,405 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16N | G16N | 1 | 1 | 0 | 0 | 16 | G | N | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,672 | MegaScale | null | null | null | null | 0.136409 | null | null | null | null | null | null | -0.565868 | -1.864636 | 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":2364900,"numValue":-0.5658676641765481,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364901,"numValue":-1.8646361234668207,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364902,"numValue":0.1364086818262388,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,553 | train | mutant | 476,053 | 358 | 477,405 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16N | G16N | 1 | 1 | 0 | 0 | 16 | G | N | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,456 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.049304 | 0.135326 | 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":12123594,"numValue":-1.0493038634345,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123595,"numValue":0.135325979720329,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,554 | train | mutant | 476,054 | 358 | 477,406 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16H | G16H | 1 | 1 | 0 | 0 | 16 | G | H | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,673 | MegaScale | null | null | null | null | 0.127403 | null | null | null | null | null | null | -0.723035 | -1.698741 | 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":2364903,"numValue":-0.7230350859584902,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364904,"numValue":-1.6987410147354236,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364905,"numValue":0.1274030670192963,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,555 | train | mutant | 476,054 | 358 | 477,406 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16H | G16H | 1 | 1 | 0 | 0 | 16 | G | H | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,451 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.741392 | 0.118438 | 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":12123584,"numValue":-0.741392081765893,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123585,"numValue":0.118438009329417,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,556 | train | mutant | 476,055 | 358 | 477,407 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16D | G16D | 1 | 1 | 0 | 0 | 16 | G | D | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,674 | MegaScale | null | null | null | null | 0.070342 | null | null | null | null | null | null | -0.643743 | -1.795286 | 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":2364906,"numValue":-0.6437425658243465,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364907,"numValue":-1.7952856062024782,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364908,"numValue":0.0703415906173761,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,557 | train | mutant | 476,055 | 358 | 477,407 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16D | G16D | 1 | 1 | 0 | 0 | 16 | G | D | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,064,429 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.755677 | 0.085712 | 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":12121540,"numValue":-0.755676566723584,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121541,"numValue":0.0857118778786418,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,558 | train | mutant | 476,056 | 358 | 477,408 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16R | G16R | 1 | 1 | 0 | 0 | 16 | G | R | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,675 | MegaScale | null | null | null | null | 0.142253 | null | null | null | null | null | null | -0.732494 | -1.949293 | 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":2364909,"numValue":-0.7324940232713393,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364910,"numValue":-1.9492927472003176,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364911,"numValue":0.1422528959816965,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,559 | train | mutant | 476,056 | 358 | 477,408 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16R | G16R | 1 | 1 | 0 | 0 | 16 | G | R | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,459 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.826133 | 0.047707 | 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":12123600,"numValue":-0.826133149753682,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123601,"numValue":0.0477070933830425,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,560 | train | mutant | 476,057 | 358 | 477,409 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16K | G16K | 1 | 1 | 0 | 0 | 16 | G | K | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,676 | MegaScale | null | null | null | null | 0.090939 | null | null | null | null | null | null | -0.73759 | -1.90917 | 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":2364912,"numValue":-0.7375901619238385,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364913,"numValue":-1.9091698691640344,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364914,"numValue":0.0909387531372747,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,562 | train | mutant | 476,058 | 358 | 477,410 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16T | G16T | 1 | 1 | 0 | 0 | 16 | G | T | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,677 | MegaScale | null | null | null | null | 0.645954 | null | null | null | null | null | null | -0.43438 | -1.596642 | 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":2364915,"numValue":-0.4343799591329861,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364916,"numValue":-1.5966421449734398,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364917,"numValue":0.6459536710643795,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,563 | train | mutant | 476,058 | 358 | 477,410 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16T | G16T | 1 | 1 | 0 | 0 | 16 | G | T | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,461 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.917266 | 0.073693 | 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":12123604,"numValue":-0.917265689531096,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123605,"numValue":0.0736925546646379,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,564 | train | mutant | 476,059 | 358 | 477,411 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16S | G16S | 1 | 1 | 0 | 0 | 16 | G | S | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,678 | MegaScale | null | null | null | null | 0.643169 | null | null | null | null | null | null | -0.433579 | -1.587872 | 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":2364918,"numValue":-0.4335790895969467,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364919,"numValue":-1.587871886096819,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364920,"numValue":0.6431691257886192,"references":[],"strValue":null,"... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,565 | train | mutant | 476,059 | 358 | 477,411 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16S | G16S | 1 | 1 | 0 | 0 | 16 | G | S | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,460 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.830283 | 0.043922 | 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":12123602,"numValue":-0.830283135097691,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123603,"numValue":0.0439224375154603,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,566 | train | mutant | 476,060 | 358 | 477,412 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16A | G16A | 1 | 1 | 0 | 0 | 16 | G | A | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,679 | MegaScale | null | null | null | null | 1.835259 | null | null | null | null | null | null | 0.299713 | -0.856353 | 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":2364921,"numValue":0.2997128468134858,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364922,"numValue":-0.856352627604867,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364923,"numValue":1.8352592488223607,"references":[],"strValue":null,"t... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,567 | train | mutant | 476,060 | 358 | 477,412 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16A | G16A | 1 | 1 | 0 | 0 | 16 | G | A | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,064,427 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.595317 | 0.036963 | 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":12121536,"numValue":-0.595316658031725,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121537,"numValue":0.0369632001839068,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,568 | train | mutant | 476,061 | 358 | 477,413 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16M | G16M | 1 | 1 | 0 | 0 | 16 | G | M | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,680 | MegaScale | null | null | null | null | 1.492132 | null | null | null | null | null | null | -0.026953 | -0.954761 | 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":2364924,"numValue":-0.0269534628647381,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364925,"numValue":-0.9547612001587508,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364926,"numValue":1.4921324807404563,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,569 | train | mutant | 476,061 | 358 | 477,413 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16M | G16M | 1 | 1 | 0 | 0 | 16 | G | M | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,455 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.780707 | 0.05162 | 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":12123592,"numValue":-0.780706692927029,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123593,"numValue":0.0516202950788562,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,570 | train | mutant | 476,062 | 358 | 477,414 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16L | G16L | 1 | 1 | 0 | 0 | 16 | G | L | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,681 | MegaScale | null | null | null | null | 1.622317 | null | null | null | null | null | null | 0.001191 | -0.838027 | 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":2364927,"numValue":0.0011907946497433,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364928,"numValue":-0.8380268227856367,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364929,"numValue":1.622316945188945,"references":[],"strValue":null,"t... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,571 | train | mutant | 476,062 | 358 | 477,414 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16L | G16L | 1 | 1 | 0 | 0 | 16 | G | L | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,454 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.744874 | 0.034944 | 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":12123590,"numValue":-0.744873761286631,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123591,"numValue":0.0349436359234743,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,572 | train | mutant | 476,063 | 358 | 477,415 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16V | G16V | 1 | 1 | 0 | 0 | 16 | G | V | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,682 | MegaScale | null | null | null | null | 1.575378 | null | null | null | null | null | null | -0.008182 | -0.900541 | 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":2364930,"numValue":-0.0081820946592169,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364931,"numValue":-0.9005407736075115,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364932,"numValue":1.5753776937467705,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,574 | train | mutant | 476,064 | 358 | 477,416 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16I | G16I | 1 | 1 | 0 | 0 | 16 | G | I | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,683 | MegaScale | null | null | null | null | 1.456306 | null | null | null | null | null | null | -0.02434 | -1.011455 | 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":2364933,"numValue":-0.0243402277645656,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364934,"numValue":-1.0114547981990205,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364935,"numValue":1.456306139570705,"references":[],"strValue":null,"... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,575 | train | mutant | 476,064 | 358 | 477,416 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16I | G16I | 1 | 1 | 0 | 0 | 16 | G | I | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,452 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.979425 | 0.101689 | 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":12123586,"numValue":-0.979425491291569,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123587,"numValue":0.101689391988291,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,576 | train | mutant | 476,065 | 358 | 477,417 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16W | G16W | 1 | 1 | 0 | 0 | 16 | G | W | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,684 | MegaScale | null | null | null | null | 2.154909 | null | null | null | null | null | null | 0.433401 | -0.570908 | 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":2364936,"numValue":0.433401381874954,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364937,"numValue":-0.5709075795772163,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364938,"numValue":2.1549086045713697,"references":[],"strValue":null,"t... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,577 | train | mutant | 476,065 | 358 | 477,417 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16W | G16W | 1 | 1 | 0 | 0 | 16 | G | W | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,463 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.916128 | 0.080751 | 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":12123608,"numValue":-0.916128477869086,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123609,"numValue":0.0807512282480899,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,578 | train | mutant | 476,066 | 358 | 477,418 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16Y | G16Y | 1 | 1 | 0 | 0 | 16 | G | Y | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,685 | MegaScale | null | null | null | null | 1.563821 | null | null | null | null | null | null | 0.032615 | -0.997682 | 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":2364939,"numValue":0.0326149567239169,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364940,"numValue":-0.9976822011098884,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364941,"numValue":1.5638212388862471,"references":[],"strValue":null,"... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,579 | train | mutant | 476,066 | 358 | 477,418 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16Y | G16Y | 1 | 1 | 0 | 0 | 16 | G | Y | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,464 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.75417 | 0.079895 | 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":12123610,"numValue":-0.754170241217553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123611,"numValue":0.079894501399756,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,580 | train | mutant | 476,067 | 358 | 477,419 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16F | G16F | 1 | 1 | 0 | 0 | 16 | G | F | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,686 | MegaScale | null | null | null | null | 1.773542 | null | null | null | null | null | null | 0.063573 | -0.749508 | 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":2364942,"numValue":0.0635734152557511,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364943,"numValue":-0.7495082400833237,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364944,"numValue":1.773541981458973,"references":[],"strValue":null,"t... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,581 | train | mutant | 476,067 | 358 | 477,419 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16F | G16F | 1 | 1 | 0 | 0 | 16 | G | F | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,064,431 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.093117 | 0.131238 | 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":12121544,"numValue":-1.09311657882375,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121545,"numValue":0.131238004030076,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,582 | train | mutant | 476,068 | 358 | 477,420 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16P | G16P | 1 | 1 | 0 | 0 | 16 | G | P | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,687 | MegaScale | null | null | null | null | -0.17423 | null | null | null | null | null | null | -0.732741 | -1.916593 | 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":2364945,"numValue":-0.7327408866710381,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364946,"numValue":-1.916592833221164,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364947,"numValue":-0.1742303025783437,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,583 | train | mutant | 476,068 | 358 | 477,420 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16P | G16P | 1 | 1 | 0 | 0 | 16 | G | P | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,065,457 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.937326 | 0.065311 | 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":12123596,"numValue":-0.937325781853718,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123597,"numValue":0.0653108244628146,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,584 | train | mutant | 476,069 | 358 | 477,421 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16C | G16C | 1 | 1 | 0 | 0 | 16 | G | C | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,688 | MegaScale | null | null | null | null | 1.397049 | null | null | null | null | null | null | -0.007798 | -1.001511 | 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":2364948,"numValue":-0.0077981874705197,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364949,"numValue":-1.0015111709144218,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364950,"numValue":1.397048672001242,"references":[],"strValue":null,"... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,585 | train | mutant | 476,069 | 358 | 477,421 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G16C | G16C | 1 | 1 | 0 | 0 | 16 | G | C | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,064,428 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.564089 | 0.058288 | 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":12121538,"numValue":-0.564088878540998,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121539,"numValue":0.0582884121130921,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,587 | train | mutant | 476,070 | 358 | 477,422 | 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 | insG16 | insG16 | 1 | 0 | 0 | 1 | 16 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,711 | MegaScale | null | null | null | null | 0.457174 | null | null | null | null | null | null | -0.537577 | -1.614841 | 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":2365017,"numValue":-0.5375765419020883,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365018,"numValue":-1.6148407447636504,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365019,"numValue":0.4571739709072091,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,588 | train | mutant | 476,071 | 358 | 477,423 | 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 | insA16 | insA16 | 1 | 0 | 0 | 1 | 16 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,690 | MegaScale | null | null | null | null | 0.464816 | null | null | null | null | null | null | -0.604615 | -1.632635 | 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":2364954,"numValue":-0.6046147622732898,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364955,"numValue":-1.632634979187847,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364956,"numValue":0.4648155534200943,"references":[],"strValue":null,"... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,589 | train | mutant | 476,072 | 358 | 477,424 | 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 | delG16 | delG16 | 1 | 0 | 1 | 0 | 16 | G | - | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 501,691 | MegaScale | null | null | null | null | 0.870139 | null | null | null | null | null | null | -0.408586 | -1.346899 | 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":2364957,"numValue":-0.4085864816076409,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364958,"numValue":-1.3468988510269346,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364959,"numValue":0.8701394933582096,"references":[],"strValue":null,... | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,590 | train | mutant | 476,072 | 358 | 477,424 | 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 | delG16 | delG16 | 1 | 0 | 1 | 0 | 16 | G | - | 9 | CONSERVATION | 1CSP | 247 | null | 16 | A | E | false | false | 0 | 16.3225 | 5,064,426 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.083647 | 0.100639 | 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":12121534,"numValue":-1.08364663133323,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121535,"numValue":0.100639459987305,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20824,"numValue":9.0,"position":16,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,591 | train | mutant | 1,767 | 358 | 1,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17A | F17A | 1 | 1 | 0 | 0 | 17 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 3,370 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | null | 1CSP_A:F17A | 48.6 | -11.3 | 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:F17A",... | [{"datasets":[],"id":12424,"numValue":48.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12425,"numValue":-11.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12426,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,593 | train | mutant | 1,767 | 358 | 1,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17A | F17A | 1 | 1 | 0 | 0 | 17 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 7,874 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F17A | null | null | 15.03 | -0.55 | null | -0.91 | -3.42 | 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":26917,"numValue":-0.91,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26918,"numValue":-3.42,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26919,"numValue":15.03,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":2... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,594 | train | mutant | 1,767 | 358 | 1,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17A | F17A | 1 | 1 | 0 | 0 | 17 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 7,877 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F17A | null | null | 14.58 | 0.81 | null | 0.1 | 33.22 | 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":26932,"numValue":0.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26933,"numValue":33.22,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26934,"numValue":14.58,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":26935,"numValue":0.81,"references"... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:18595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,595 | train | mutant | 1,767 | 358 | 1,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17A | F17A | 1 | 1 | 0 | 0 | 17 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 10,700 | ProTherm | 7 | CD | Urea | Potassium phosphate | 0.35 M | 25 | 1CSP_A:F17A | null | null | 1.96 | 1.53 | null | null | null | 2.57 | 0.76 | 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":36737,"numValue":1.96,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":36738,"numValue":1.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36739,"numValue":0.76,"references":[],"strValue":... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,596 | train | mutant | 1,767 | 358 | 1,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17A | F17A | 1 | 1 | 0 | 0 | 17 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,701 | MegaScale | null | null | null | null | 4.176376 | null | null | null | null | null | null | 1.904779 | 0.896721 | 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":2364987,"numValue":1.9047791586468237,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364988,"numValue":0.8967207663180286,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364989,"numValue":4.17637617059736,"references":[],"strValue":null,"typ... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,597 | train | mutant | 1,767 | 358 | 1,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17A | F17A | 1 | 1 | 0 | 0 | 17 | F | A | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,064,433 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.189657 | 0.035165 | 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":12121548,"numValue":-0.18965692469041,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121549,"numValue":0.0351651594313586,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,598 | train | mutant | 476,073 | 358 | 477,425 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17Q | F17Q | 1 | 1 | 0 | 0 | 17 | F | Q | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,692 | MegaScale | null | null | null | null | 4.002953 | null | null | null | null | null | null | 1.767678 | 0.859495 | 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":2364960,"numValue":1.7676775359516772,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364961,"numValue":0.8594948308751686,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364962,"numValue":4.002953477681875,"references":[],"strValue":null,"ty... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,599 | train | mutant | 476,073 | 358 | 477,425 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17Q | F17Q | 1 | 1 | 0 | 0 | 17 | F | Q | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,444 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.20112 | 0.049951 | 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":12123570,"numValue":-0.201119817064775,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123571,"numValue":0.0499510025599376,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,600 | train | mutant | 476,074 | 358 | 477,426 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17E | F17E | 1 | 1 | 0 | 0 | 17 | F | E | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,693 | MegaScale | null | null | null | null | 3.23338 | null | null | null | null | null | null | 1.301782 | 0.398239 | 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":2364963,"numValue":1.3017823389748386,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364964,"numValue":0.3982387267668404,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364965,"numValue":3.2333797161310733,"references":[],"strValue":null,"t... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,601 | train | mutant | 476,074 | 358 | 477,426 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17E | F17E | 1 | 1 | 0 | 0 | 17 | F | E | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,064,436 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.212088 | 0.046501 | 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":12121554,"numValue":-0.212088349588225,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121555,"numValue":0.0465007020093888,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,602 | train | mutant | 476,075 | 358 | 477,427 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17N | F17N | 1 | 1 | 0 | 0 | 17 | F | N | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,694 | MegaScale | null | null | null | null | 2.484353 | null | null | null | null | null | null | 0.76528 | -0.281099 | 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":2364966,"numValue":0.7652797803107272,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364967,"numValue":-0.2810985410286079,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364968,"numValue":2.4843527118223108,"references":[],"strValue":null,"... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,603 | train | mutant | 476,075 | 358 | 477,427 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17N | F17N | 1 | 1 | 0 | 0 | 17 | F | N | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,442 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.394564 | 0.060514 | 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":12123566,"numValue":-0.394563562747176,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123567,"numValue":0.0605141845396256,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,604 | train | mutant | 476,076 | 358 | 477,428 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17H | F17H | 1 | 1 | 0 | 0 | 17 | F | H | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,695 | MegaScale | null | null | null | null | 4.232119 | null | null | null | null | null | null | 1.924798 | 0.93708 | 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":2364969,"numValue":1.9247978829393184,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364970,"numValue":0.937079738355292,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364971,"numValue":4.232119022290238,"references":[],"strValue":null,"typ... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,606 | train | mutant | 476,077 | 358 | 477,429 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17D | F17D | 1 | 1 | 0 | 0 | 17 | F | D | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,696 | MegaScale | null | null | null | null | 0.772184 | null | null | null | null | null | null | -0.181282 | -1.446004 | 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":2364972,"numValue":-0.1812821365212425,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364973,"numValue":-1.446003715155528,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364974,"numValue":0.7721839703905569,"references":[],"strValue":null,"... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,607 | train | mutant | 476,077 | 358 | 477,429 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17D | F17D | 1 | 1 | 0 | 0 | 17 | F | D | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,064,435 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.695685 | 0.05526 | 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":12121552,"numValue":-0.695685017455626,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121553,"numValue":0.0552601268174088,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,608 | train | mutant | 476,078 | 358 | 477,430 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17R | F17R | 1 | 1 | 0 | 0 | 17 | F | R | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,697 | MegaScale | null | null | null | null | 3.991931 | null | null | null | null | null | null | 1.786671 | 0.745547 | 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":2364975,"numValue":1.7866708391502524,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364976,"numValue":0.7455472047842606,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364977,"numValue":3.9919310957192735,"references":[],"strValue":null,"t... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,609 | train | mutant | 476,078 | 358 | 477,430 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17R | F17R | 1 | 1 | 0 | 0 | 17 | F | R | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,445 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.200832 | 0.030072 | 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":12123572,"numValue":-0.200832156059714,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123573,"numValue":0.0300715478548003,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,610 | train | mutant | 476,079 | 358 | 477,431 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17K | F17K | 1 | 1 | 0 | 0 | 17 | F | K | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,698 | MegaScale | null | null | null | null | 4.518576 | null | null | null | null | null | null | 2.112202 | 1.094027 | 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":2364978,"numValue":2.112201800036822,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364979,"numValue":1.0940265258190718,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364980,"numValue":4.518575612256986,"references":[],"strValue":null,"typ... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,611 | train | mutant | 476,079 | 358 | 477,431 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17K | F17K | 1 | 1 | 0 | 0 | 17 | F | K | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,439 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.070799 | 0.054482 | 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":12123560,"numValue":-0.0707989548275926,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123561,"numValue":0.0544818289940581,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,612 | train | mutant | 476,080 | 358 | 477,432 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17T | F17T | 1 | 1 | 0 | 0 | 17 | F | T | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,699 | MegaScale | null | null | null | null | 3.877619 | null | null | null | null | null | null | 1.623821 | 0.685992 | 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":2364981,"numValue":1.6238206234919828,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364982,"numValue":0.6859922385607935,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364983,"numValue":3.877618923606958,"references":[],"strValue":null,"ty... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,613 | train | mutant | 476,080 | 358 | 477,432 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17T | F17T | 1 | 1 | 0 | 0 | 17 | F | T | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,447 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.188307 | 0.044382 | 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":12123576,"numValue":-0.188306942020606,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123577,"numValue":0.0443824620506746,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,614 | train | mutant | 476,081 | 358 | 477,433 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17S | F17S | 1 | 1 | 0 | 0 | 17 | F | S | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,700 | MegaScale | null | null | null | null | 3.598777 | null | null | null | null | null | null | 1.609515 | 0.559927 | 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":2364984,"numValue":1.6095150795704027,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364985,"numValue":0.559927282315684,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364986,"numValue":3.5987768911299582,"references":[],"strValue":null,"ty... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,615 | train | mutant | 476,081 | 358 | 477,433 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17S | F17S | 1 | 1 | 0 | 0 | 17 | F | S | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,446 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.188316 | 0.030761 | 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":12123574,"numValue":-0.18831614226597,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123575,"numValue":0.0307614190532052,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,616 | train | mutant | 476,082 | 358 | 477,434 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17G | F17G | 1 | 1 | 0 | 0 | 17 | F | G | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,702 | MegaScale | null | null | null | null | 2.877052 | null | null | null | null | null | null | 1.125472 | 0.016016 | 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":2364990,"numValue":1.1254720994415337,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364991,"numValue":0.0160155230037105,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364992,"numValue":2.877052457911964,"references":[],"strValue":null,"ty... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,617 | train | mutant | 476,082 | 358 | 477,434 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17G | F17G | 1 | 1 | 0 | 0 | 17 | F | G | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,436 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.379598 | 0.034862 | 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":12123554,"numValue":-0.379598443637426,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123555,"numValue":0.0348618825431662,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,618 | train | mutant | 476,083 | 358 | 477,435 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17M | F17M | 1 | 1 | 0 | 0 | 17 | F | M | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,703 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.38532 | 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":2364993,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364994,"numValue":1.3853196938682122,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364995,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,619 | train | mutant | 476,083 | 358 | 477,435 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17M | F17M | 1 | 1 | 0 | 0 | 17 | F | M | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,441 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.110965 | 0.044491 | 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":12123564,"numValue":-0.110964772689844,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123565,"numValue":0.0444912334848696,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,620 | train | mutant | 476,084 | 358 | 477,436 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17L | F17L | 1 | 1 | 0 | 0 | 17 | F | L | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,704 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.015973 | 1.414146 | 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":2364996,"numValue":2.015972589780294,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364997,"numValue":1.4141463133287355,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364998,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,621 | train | mutant | 476,084 | 358 | 477,436 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17L | F17L | 1 | 1 | 0 | 0 | 17 | F | L | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,440 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.132334 | 0.028785 | 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":12123562,"numValue":-0.132333875922915,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123563,"numValue":0.0287853780868433,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,622 | train | mutant | 476,085 | 358 | 477,437 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17V | F17V | 1 | 1 | 0 | 0 | 17 | F | V | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,705 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.195205 | 1.469373 | 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":2364999,"numValue":2.19520532827122,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365000,"numValue":1.4693728550880918,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365001,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,623 | train | mutant | 476,085 | 358 | 477,437 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17V | F17V | 1 | 1 | 0 | 0 | 17 | F | V | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,448 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.157236 | 0.030292 | 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":12123578,"numValue":-0.15723648672561,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123579,"numValue":0.0302916483914015,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,625 | train | mutant | 476,086 | 358 | 477,438 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17I | F17I | 1 | 1 | 0 | 0 | 17 | F | I | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,438 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.118313 | 0.054579 | 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":12123558,"numValue":-0.118312701987553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123559,"numValue":0.0545788425146773,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,626 | train | mutant | 476,087 | 358 | 477,439 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17W | F17W | 1 | 1 | 0 | 0 | 17 | F | W | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,707 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.408946 | 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":2365005,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365006,"numValue":1.4089460491379973,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365007,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,627 | train | mutant | 476,087 | 358 | 477,439 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17W | F17W | 1 | 1 | 0 | 0 | 17 | F | W | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,449 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.105849 | 0.042578 | 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":12123580,"numValue":-0.105848822917541,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123581,"numValue":0.0425775763155753,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,628 | train | mutant | 476,088 | 358 | 477,440 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17Y | F17Y | 1 | 1 | 0 | 0 | 17 | F | Y | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,708 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.519253 | 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":2365008,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365009,"numValue":1.5192528150874225,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365010,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,630 | train | mutant | 476,089 | 358 | 477,441 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17P | F17P | 1 | 1 | 0 | 0 | 17 | F | P | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,709 | MegaScale | null | null | null | null | -0.277604 | null | null | null | null | null | null | -0.621793 | -1.866333 | 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":2365011,"numValue":-0.6217929303054812,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365012,"numValue":-1.8663333546174756,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365013,"numValue":-0.2776043718519481,"references":[],"strValue":null... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,631 | train | mutant | 476,089 | 358 | 477,441 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17P | F17P | 1 | 1 | 0 | 0 | 17 | F | P | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 5,065,443 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.882841 | 0.065209 | 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":12123568,"numValue":-0.88284057943636,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123569,"numValue":0.065208947079146,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18632 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,632 | train | mutant | 476,090 | 358 | 477,442 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F17C | F17C | 1 | 1 | 0 | 0 | 17 | F | C | 9 | CONSERVATION | 1CSP | 247 | null | 17 | A | E | true | false | 60.016307 | 21.416364 | 501,710 | MegaScale | null | null | null | null | 4.410645 | null | null | null | null | null | null | 1.810307 | 0.984065 | 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":2365014,"numValue":1.810307044248125,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365015,"numValue":0.984065007239566,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365016,"numValue":4.410645292500046,"references":[],"strValue":null,"type... | [{"id":20825,"numValue":9.0,"position":17,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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