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:20060 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,060 | train | mutant | 476,544 | 358 | 477,896 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39A | K39A | 1 | 1 | 0 | 0 | 39 | K | A | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,611 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.128194 | 0.034932 | 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":12121904,"numValue":-0.128194378858621,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121905,"numValue":0.0349322276192225,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20062 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,062 | train | mutant | 476,545 | 358 | 477,897 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39G | K39G | 1 | 1 | 0 | 0 | 39 | K | G | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,616 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.13095 | 0.040339 | 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":12121914,"numValue":-0.130949545670417,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121915,"numValue":0.0403391566184142,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20063 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,063 | train | mutant | 476,546 | 358 | 477,898 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39M | K39M | 1 | 1 | 0 | 0 | 39 | K | M | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,186 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.144309 | 1.484684 | 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":2366441,"numValue":2.144308502031578,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366442,"numValue":1.4846841385509706,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366443,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20064 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,064 | train | mutant | 476,546 | 358 | 477,898 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39M | K39M | 1 | 1 | 0 | 0 | 39 | K | M | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,179 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.125791 | 0.045959 | 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":12123040,"numValue":-0.125790661419746,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123041,"numValue":0.045958672620493,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20065 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,065 | train | mutant | 476,547 | 358 | 477,899 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39L | K39L | 1 | 1 | 0 | 0 | 39 | K | L | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,187 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.659766 | 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":2366444,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366445,"numValue":1.6597659042199615,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366446,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20066 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,066 | train | mutant | 476,547 | 358 | 477,899 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39L | K39L | 1 | 1 | 0 | 0 | 39 | K | L | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,178 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.078532 | 0.031115 | 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":12123038,"numValue":-0.078532067731225,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123039,"numValue":0.0311149108805966,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20067 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,067 | train | mutant | 476,548 | 358 | 477,900 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39V | K39V | 1 | 1 | 0 | 0 | 39 | K | V | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,188 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.154362 | 1.555797 | 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":2366447,"numValue":2.15436174735712,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366448,"numValue":1.555796869449478,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366449,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20068 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,068 | train | mutant | 476,548 | 358 | 477,900 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39V | K39V | 1 | 1 | 0 | 0 | 39 | K | V | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,186 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.117026 | 0.03043 | 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":12123054,"numValue":-0.117025894335918,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123055,"numValue":0.0304302592880617,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20069 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,069 | train | mutant | 476,549 | 358 | 477,901 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39I | K39I | 1 | 1 | 0 | 0 | 39 | K | I | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,189 | MegaScale | null | null | null | null | 4.917203 | null | null | null | null | null | null | 2.14482 | 1.362529 | 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":2366450,"numValue":2.1448195066442377,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366451,"numValue":1.362528990634353,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366452,"numValue":4.9172032955200695,"references":[],"strValue":null,"ty... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20070 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,070 | train | mutant | 476,549 | 358 | 477,901 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39I | K39I | 1 | 1 | 0 | 0 | 39 | K | I | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,618 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.164327 | 0.061369 | 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":12121918,"numValue":-0.164326809153116,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121919,"numValue":0.061368703329072,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20071 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,071 | train | mutant | 476,550 | 358 | 477,902 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39W | K39W | 1 | 1 | 0 | 0 | 39 | K | W | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,190 | MegaScale | null | null | null | null | 4.842916 | null | null | null | null | null | null | 2.041545 | 1.173618 | 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":2366453,"numValue":2.0415453692656698,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366454,"numValue":1.1736180267570937,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366455,"numValue":4.84291573087047,"references":[],"strValue":null,"typ... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20073 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,073 | train | mutant | 476,551 | 358 | 477,903 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Y | K39Y | 1 | 1 | 0 | 0 | 39 | K | Y | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,191 | MegaScale | null | null | null | null | 4.755322 | null | null | null | null | null | null | 2.020474 | 1.278253 | 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":2366456,"numValue":2.0204735466884824,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366457,"numValue":1.2782526117958224,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366458,"numValue":4.7553217382460256,"references":[],"strValue":null,"t... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20074 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,074 | train | mutant | 476,551 | 358 | 477,903 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Y | K39Y | 1 | 1 | 0 | 0 | 39 | K | Y | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,188 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.310749 | 0.081297 | 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":12123058,"numValue":-0.310748714127707,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123059,"numValue":0.0812967414632303,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20075 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,075 | train | mutant | 476,552 | 358 | 477,904 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39F | K39F | 1 | 1 | 0 | 0 | 39 | K | F | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,192 | MegaScale | null | null | null | null | 4.726022 | null | null | null | null | null | null | 2.067846 | 1.182529 | 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":2366459,"numValue":2.067846443630845,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366460,"numValue":1.1825286835653273,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366461,"numValue":4.726021760963993,"references":[],"strValue":null,"typ... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20076 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,076 | train | mutant | 476,552 | 358 | 477,904 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39F | K39F | 1 | 1 | 0 | 0 | 39 | K | F | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,615 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.287938 | 0.067707 | 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":12121912,"numValue":-0.287938239120879,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121913,"numValue":0.0677074270452744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20077 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,077 | train | mutant | 476,553 | 358 | 477,905 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39P | K39P | 1 | 1 | 0 | 0 | 39 | K | P | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,193 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.228648 | 1.613516 | 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":2366462,"numValue":2.2286479384013766,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366463,"numValue":1.6135157642790718,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366464,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20078 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,078 | train | mutant | 476,553 | 358 | 477,905 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39P | K39P | 1 | 1 | 0 | 0 | 39 | K | P | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,181 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.106279 | 0.047847 | 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":12123044,"numValue":-0.106278781050905,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123045,"numValue":0.0478473419233775,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20079 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,079 | train | mutant | 476,554 | 358 | 477,906 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39C | K39C | 1 | 1 | 0 | 0 | 39 | K | C | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,194 | MegaScale | null | null | null | null | 4.531142 | null | null | null | null | null | null | 1.823381 | 1.076411 | 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":2366465,"numValue":1.8233809721728904,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366466,"numValue":1.0764114125774014,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366467,"numValue":4.531141863004829,"references":[],"strValue":null,"ty... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20080 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,080 | train | mutant | 476,554 | 358 | 477,906 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39C | K39C | 1 | 1 | 0 | 0 | 39 | K | C | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,612 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.123996 | 0.053361 | 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":12121906,"numValue":-0.123996000223995,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121907,"numValue":0.0533607361619263,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20081 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,081 | train | mutant | 476,555 | 358 | 477,907 | 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 | insG39 | insG39 | 1 | 0 | 0 | 1 | 39 | - | G | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,195 | MegaScale | null | null | null | null | 4.514862 | null | null | null | null | null | null | 1.775219 | 1.084561 | 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":2366468,"numValue":1.7752191639972037,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366469,"numValue":1.08456113462266,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366470,"numValue":4.51486175711338,"references":[],"strValue":null,"type"... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20082 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,082 | train | mutant | 476,556 | 358 | 477,908 | 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 | insA39 | insA39 | 1 | 0 | 0 | 1 | 39 | - | A | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,196 | MegaScale | null | null | null | null | 4.645869 | null | null | null | null | null | null | 1.705369 | 1.147628 | 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":2366471,"numValue":1.7053693320905878,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366472,"numValue":1.147627871517216,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366473,"numValue":4.645868723300745,"references":[],"strValue":null,"typ... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20083 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,083 | train | mutant | 476,557 | 358 | 477,909 | 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 | delK39 | delK39 | 1 | 0 | 1 | 0 | 39 | K | - | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,197 | MegaScale | null | null | null | null | 4.775105 | null | null | null | null | null | null | 1.83454 | 1.207973 | 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":2366474,"numValue":1.834539685720057,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366475,"numValue":1.2079730140997762,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366476,"numValue":4.775105387996605,"references":[],"strValue":null,"typ... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20084 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,084 | train | mutant | 476,557 | 358 | 477,909 | 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 | delK39 | delK39 | 1 | 0 | 1 | 0 | 39 | K | - | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,610 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.986269 | 0.089521 | 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":12121902,"numValue":-0.986269001803432,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121903,"numValue":0.0895205954546004,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20085 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,085 | train | mutant | 476,558 | 358 | 477,910 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40Q | T40Q | 1 | 1 | 0 | 0 | 40 | T | Q | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,198 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.524865 | 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":2366477,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366478,"numValue":1.5248653072953542,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366479,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20086 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,086 | train | mutant | 476,558 | 358 | 477,910 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40Q | T40Q | 1 | 1 | 0 | 0 | 40 | T | Q | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,633 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.036759 | 0.040416 | 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":12121948,"numValue":-0.0367586603289652,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121949,"numValue":0.0404155002544481,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20087 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,087 | train | mutant | 476,559 | 358 | 477,911 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40E | T40E | 1 | 1 | 0 | 0 | 40 | T | E | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,199 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.157652 | 1.525831 | 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":2366480,"numValue":2.157651697759994,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366481,"numValue":1.5258311282497556,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366482,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20088 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,088 | train | mutant | 476,559 | 358 | 477,911 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40E | T40E | 1 | 1 | 0 | 0 | 40 | T | E | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,623 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.060443 | 0.037974 | 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":12121928,"numValue":-0.0604431586454123,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121929,"numValue":0.0379742458144864,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20089 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,089 | train | mutant | 476,560 | 358 | 477,912 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40N | T40N | 1 | 1 | 0 | 0 | 40 | T | N | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,200 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.50963 | 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":2366483,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366484,"numValue":1.509629583851242,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366485,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20090 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,090 | train | mutant | 476,560 | 358 | 477,912 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40N | T40N | 1 | 1 | 0 | 0 | 40 | T | N | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,631 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.065559 | 0.05634 | 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":12121944,"numValue":-0.0655591084177154,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121945,"numValue":0.0563397694774255,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20091 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,091 | train | mutant | 476,561 | 358 | 477,913 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40H | T40H | 1 | 1 | 0 | 0 | 40 | T | H | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,201 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.168189 | 1.688929 | 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":2366486,"numValue":2.1681889282286484,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366487,"numValue":1.6889294811889737,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366488,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20092 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,092 | train | mutant | 476,561 | 358 | 477,913 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40H | T40H | 1 | 1 | 0 | 0 | 40 | T | H | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,626 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.06939 | 0.066277 | 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":12121934,"numValue":-0.0693900905874559,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121935,"numValue":0.0662772795708613,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20093 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,093 | train | mutant | 476,562 | 358 | 477,914 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40D | T40D | 1 | 1 | 0 | 0 | 40 | T | D | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,202 | MegaScale | null | null | null | null | 4.977541 | null | null | null | null | null | null | null | 1.421104 | 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":2366489,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366490,"numValue":1.421103989954599,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366491,"numValue":4.977540880639384,"references":[],"strValue":null,"type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20094 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,094 | train | mutant | 476,562 | 358 | 477,914 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40D | T40D | 1 | 1 | 0 | 0 | 40 | T | D | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,622 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.052408 | 0.076616 | 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":12121926,"numValue":-0.0524076643441362,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121927,"numValue":0.0766156566218183,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20097 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,097 | train | mutant | 476,564 | 358 | 477,916 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40K | T40K | 1 | 1 | 0 | 0 | 40 | T | K | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,204 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.169428 | 1.55116 | 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":2366495,"numValue":2.1694276009552858,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366496,"numValue":1.5511595000512313,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366497,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20098 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,098 | train | mutant | 476,564 | 358 | 477,916 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40K | T40K | 1 | 1 | 0 | 0 | 40 | T | K | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,628 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.071642 | 0.05467 | 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":12121938,"numValue":-0.0716423106526635,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121939,"numValue":0.0546704769585068,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20099 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,099 | train | mutant | 476,565 | 358 | 477,917 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40S | T40S | 1 | 1 | 0 | 0 | 40 | T | S | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,205 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.701653 | 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":2366498,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366499,"numValue":1.7016531239145634,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366500,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20100 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,100 | train | mutant | 476,565 | 358 | 477,917 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40S | T40S | 1 | 1 | 0 | 0 | 40 | T | S | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,635 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.01541 | 0.035484 | 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":12121952,"numValue":-0.0154097976356964,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121953,"numValue":0.0354843282100438,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20101 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,101 | train | mutant | 476,566 | 358 | 477,918 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40A | T40A | 1 | 1 | 0 | 0 | 40 | T | A | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,206 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.612654 | 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":2366501,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366502,"numValue":1.6126535332520442,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366503,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20102 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,102 | train | mutant | 476,566 | 358 | 477,918 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40A | T40A | 1 | 1 | 0 | 0 | 40 | T | A | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,620 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.059269 | 0.032238 | 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":12121922,"numValue":-0.0592685939872225,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121923,"numValue":0.0322382301721065,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20103 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,103 | train | mutant | 476,567 | 358 | 477,919 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40G | T40G | 1 | 1 | 0 | 0 | 40 | T | G | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,207 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.43231 | 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":2366504,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366505,"numValue":1.4323104762369332,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366506,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20104 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,104 | train | mutant | 476,567 | 358 | 477,919 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40G | T40G | 1 | 1 | 0 | 0 | 40 | T | G | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,625 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.089406 | 0.039644 | 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":12121932,"numValue":-0.0894055310525761,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121933,"numValue":0.0396439492776979,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20105 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,105 | train | mutant | 476,568 | 358 | 477,920 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40M | T40M | 1 | 1 | 0 | 0 | 40 | T | M | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,208 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.223597 | 1.562422 | 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":2366507,"numValue":2.223596652161977,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366508,"numValue":1.5624219621663835,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366509,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20107 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,107 | train | mutant | 476,569 | 358 | 477,921 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40L | T40L | 1 | 1 | 0 | 0 | 40 | T | L | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,209 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.237943 | 1.467839 | 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":2366510,"numValue":2.2379433801028465,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366511,"numValue":1.4678391416582213,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366512,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20110 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,110 | train | mutant | 476,570 | 358 | 477,922 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40V | T40V | 1 | 1 | 0 | 0 | 40 | T | V | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,065,175 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.026951 | 0.034561 | 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":12123032,"numValue":-0.0269511987705036,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123033,"numValue":0.034560691043923,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20111 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,111 | train | mutant | 476,571 | 358 | 477,923 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40I | T40I | 1 | 1 | 0 | 0 | 40 | T | I | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,211 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.620569 | 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":2366516,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366517,"numValue":1.6205690347889228,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366518,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20112 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,112 | train | mutant | 476,571 | 358 | 477,923 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40I | T40I | 1 | 1 | 0 | 0 | 40 | T | I | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,627 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.057924 | 0.052376 | 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":12121936,"numValue":-0.0579235181149458,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121937,"numValue":0.0523760277670765,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20113 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,113 | train | mutant | 476,572 | 358 | 477,924 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40W | T40W | 1 | 1 | 0 | 0 | 40 | T | W | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,212 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.092315 | 1.58556 | 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":2366519,"numValue":2.0923150733463896,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366520,"numValue":1.585560156250058,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366521,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20114 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,114 | train | mutant | 476,572 | 358 | 477,924 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40W | T40W | 1 | 1 | 0 | 0 | 40 | T | W | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,065,176 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.029873 | 0.060006 | 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":12123034,"numValue":-0.0298725833485495,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123035,"numValue":0.0600064781994359,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20115 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,115 | train | mutant | 476,573 | 358 | 477,925 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40Y | T40Y | 1 | 1 | 0 | 0 | 40 | T | Y | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,213 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.209292 | 1.661714 | 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":2366522,"numValue":2.2092922207629613,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366523,"numValue":1.6617140300380029,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366524,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20116 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,116 | train | mutant | 476,573 | 358 | 477,925 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40Y | T40Y | 1 | 1 | 0 | 0 | 40 | T | Y | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,065,177 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.09109 | 0.056258 | 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":12123036,"numValue":-0.0910904026536451,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123037,"numValue":0.0562578566261977,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20117 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,117 | train | mutant | 476,574 | 358 | 477,926 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40F | T40F | 1 | 1 | 0 | 0 | 40 | T | F | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,214 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.715564 | 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":2366525,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366526,"numValue":1.7155643877509732,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366527,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20118 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,118 | train | mutant | 476,574 | 358 | 477,926 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40F | T40F | 1 | 1 | 0 | 0 | 40 | T | F | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,624 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.009807 | 0.054352 | 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":12121930,"numValue":-0.00980684820877041,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121931,"numValue":0.0543521975368735,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20119 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,119 | train | mutant | 476,575 | 358 | 477,927 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40P | T40P | 1 | 1 | 0 | 0 | 40 | T | P | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,215 | MegaScale | null | null | null | null | 3.605821 | null | null | null | null | null | null | 1.568871 | 0.631616 | 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":2366528,"numValue":1.568870536592358,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366529,"numValue":0.631615515747193,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366530,"numValue":3.605820579829464,"references":[],"strValue":null,"type... | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20120 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,120 | train | mutant | 476,575 | 358 | 477,927 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40P | T40P | 1 | 1 | 0 | 0 | 40 | T | P | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,632 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.296847 | 0.04417 | 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":12121946,"numValue":-0.296846530032392,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121947,"numValue":0.0441704761304848,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20121 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,121 | train | mutant | 476,576 | 358 | 477,928 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40C | T40C | 1 | 1 | 0 | 0 | 40 | T | C | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,216 | MegaScale | null | null | null | null | 4.940224 | null | null | null | null | null | null | 1.973445 | 1.238303 | 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":2366531,"numValue":1.9734451100971293,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366532,"numValue":1.238302562153705,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366533,"numValue":4.94022409125384,"references":[],"strValue":null,"type... | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20122 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,122 | train | mutant | 476,576 | 358 | 477,928 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | T40C | T40C | 1 | 1 | 0 | 0 | 40 | T | C | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,621 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.016187 | 0.076722 | 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":12121924,"numValue":-0.0161869116941435,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121925,"numValue":0.0767224408030146,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20123 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,123 | train | mutant | 476,577 | 358 | 477,929 | 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 | insG40 | insG40 | 1 | 0 | 0 | 1 | 40 | - | G | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,217 | MegaScale | null | null | null | null | 4.473339 | null | null | null | null | null | null | 1.716646 | 1.049582 | 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":2366534,"numValue":1.7166461804903117,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366535,"numValue":1.0495816835350902,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366536,"numValue":4.473338968528093,"references":[],"strValue":null,"ty... | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20125 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,125 | train | mutant | 476,579 | 358 | 477,931 | 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 | delT40 | delT40 | 1 | 0 | 1 | 0 | 40 | T | - | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 502,219 | MegaScale | null | null | null | null | 4.523541 | null | null | null | null | null | null | 1.755599 | 1.020021 | 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":2366540,"numValue":1.7555990904158727,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366541,"numValue":1.0200206162535888,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366542,"numValue":4.523541206888881,"references":[],"strValue":null,"ty... | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20126 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,126 | train | mutant | 476,579 | 358 | 477,931 | 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 | delT40 | delT40 | 1 | 0 | 1 | 0 | 40 | T | - | 4 | CONSERVATION | 1CSP | 247 | null | 40 | A | L | true | true | 36.029201 | 18.717143 | 5,064,619 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.865976 | 0.077045 | 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":12121920,"numValue":-0.865976468348427,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121921,"numValue":0.0770446947306453,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20848,"numValue":4.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,127 | train | mutant | 476,580 | 358 | 477,932 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41Q | L41Q | 1 | 1 | 0 | 0 | 41 | L | Q | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,220 | MegaScale | null | null | null | null | 1.281917 | null | null | null | null | null | null | 0.014129 | -1.151932 | 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":2366543,"numValue":0.0141292847004252,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366544,"numValue":-1.1519317111836034,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366545,"numValue":1.281917134743332,"references":[],"strValue":null,"t... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,128 | train | mutant | 476,580 | 358 | 477,932 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41Q | L41Q | 1 | 1 | 0 | 0 | 41 | L | Q | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,168 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.891824 | 0.066723 | 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":12123018,"numValue":-0.891823637675201,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123019,"numValue":0.0667234301360661,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,129 | train | mutant | 476,581 | 358 | 477,933 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41E | L41E | 1 | 1 | 0 | 0 | 41 | L | E | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,221 | MegaScale | null | null | null | null | 1.075613 | null | null | null | null | null | null | -0.010617 | -1.258535 | 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":2366546,"numValue":-0.0106172774604567,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366547,"numValue":-1.258534515494636,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366548,"numValue":1.0756134329566271,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,130 | train | mutant | 476,581 | 358 | 477,933 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41E | L41E | 1 | 1 | 0 | 0 | 41 | L | E | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,640 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.911582 | 0.082819 | 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":12121962,"numValue":-0.911581777944963,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121963,"numValue":0.0828190753961948,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20131 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,131 | train | mutant | 476,582 | 358 | 477,934 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41N | L41N | 1 | 1 | 0 | 0 | 41 | L | N | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,222 | MegaScale | null | null | null | null | 1.438938 | null | null | null | null | null | null | 0.167794 | -1.072827 | 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":2366549,"numValue":0.1677944922085286,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366550,"numValue":-1.0728271459388656,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366551,"numValue":1.4389377278390574,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,132 | train | mutant | 476,582 | 358 | 477,934 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41N | L41N | 1 | 1 | 0 | 0 | 41 | L | N | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,166 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.685443 | 0.100611 | 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":12123014,"numValue":-0.685442997641118,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123015,"numValue":0.100610755221768,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20133 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,133 | train | mutant | 476,583 | 358 | 477,935 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41H | L41H | 1 | 1 | 0 | 0 | 41 | L | H | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,223 | MegaScale | null | null | null | null | 1.622895 | null | null | null | null | null | null | 0.066731 | -0.950229 | 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":2366552,"numValue":0.0667311846474458,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366553,"numValue":-0.9502285206557894,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366554,"numValue":1.6228949905841237,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,134 | train | mutant | 476,583 | 358 | 477,935 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41H | L41H | 1 | 1 | 0 | 0 | 41 | L | H | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,643 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.008579 | 0.196583 | 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":12121968,"numValue":-1.00857898346244,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121969,"numValue":0.196582808065769,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20135 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,135 | train | mutant | 476,584 | 358 | 477,936 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41D | L41D | 1 | 1 | 0 | 0 | 41 | L | D | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,224 | MegaScale | null | null | null | null | 1.126315 | null | null | null | null | null | null | -0.04231 | -1.250659 | 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":2366555,"numValue":-0.0423100384453082,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366556,"numValue":-1.2506592886299863,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366557,"numValue":1.1263145989034606,"references":[],"strValue":null,... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20136 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,136 | train | mutant | 476,584 | 358 | 477,936 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41D | L41D | 1 | 1 | 0 | 0 | 41 | L | D | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,639 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.659976 | 0.177156 | 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":12121960,"numValue":-0.659975921117832,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121961,"numValue":0.177155753959188,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,138 | train | mutant | 476,585 | 358 | 477,937 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41R | L41R | 1 | 1 | 0 | 0 | 41 | L | R | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,169 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.930036 | 0.052755 | 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":12123020,"numValue":-0.93003618211162,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123021,"numValue":0.0527552189465192,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20139 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,139 | train | mutant | 476,586 | 358 | 477,938 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41K | L41K | 1 | 1 | 0 | 0 | 41 | L | K | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,226 | MegaScale | null | null | null | null | 0.865237 | null | null | null | null | null | null | -0.062689 | -1.463986 | 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":2366561,"numValue":-0.0626889078538381,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366562,"numValue":-1.4639859463925902,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366563,"numValue":0.865237485942183,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,140 | train | mutant | 476,586 | 358 | 477,938 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41K | L41K | 1 | 1 | 0 | 0 | 41 | L | K | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,645 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.63839 | 0.061248 | 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":12121972,"numValue":-0.638390305443853,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121973,"numValue":0.0612477262360269,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,142 | train | mutant | 476,587 | 358 | 477,939 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41T | L41T | 1 | 1 | 0 | 0 | 41 | L | T | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,171 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.636102 | 0.045312 | 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":12123024,"numValue":-0.636101529737064,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123025,"numValue":0.045311895371375,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20143 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,143 | train | mutant | 476,588 | 358 | 477,940 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41S | L41S | 1 | 1 | 0 | 0 | 41 | L | S | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,228 | MegaScale | null | null | null | null | 2.699832 | null | null | null | null | null | null | 0.914527 | -0.083066 | 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":2366567,"numValue":0.9145271299763902,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366568,"numValue":-0.083066073712876,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366569,"numValue":2.699831919767199,"references":[],"strValue":null,"ty... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20144 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,144 | train | mutant | 476,588 | 358 | 477,940 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41S | L41S | 1 | 1 | 0 | 0 | 41 | L | S | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,170 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.815313 | 0.045572 | 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":12123022,"numValue":-0.815313293195321,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123023,"numValue":0.0455724033856167,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,145 | train | mutant | 476,589 | 358 | 477,941 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41A | L41A | 1 | 1 | 0 | 0 | 41 | L | A | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,229 | MegaScale | null | null | null | null | 4.450653 | null | null | null | null | null | null | 1.850673 | 1.021597 | 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":2366570,"numValue":1.850673208046044,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366571,"numValue":1.0215969923949495,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366572,"numValue":4.450652518132641,"references":[],"strValue":null,"typ... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20146 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,146 | train | mutant | 476,589 | 358 | 477,941 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41A | L41A | 1 | 1 | 0 | 0 | 41 | L | A | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,637 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.515254 | 0.045846 | 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":12121956,"numValue":-0.515254282821553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121957,"numValue":0.0458456384059459,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20147 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,147 | train | mutant | 476,590 | 358 | 477,942 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41G | L41G | 1 | 1 | 0 | 0 | 41 | L | G | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,230 | MegaScale | null | null | null | null | 2.449881 | null | null | null | null | null | null | 0.79586 | -0.3217 | 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":2366573,"numValue":0.7958596196702598,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366574,"numValue":-0.3217004323126937,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366575,"numValue":2.4498805975939417,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20148 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,148 | train | mutant | 476,590 | 358 | 477,942 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41G | L41G | 1 | 1 | 0 | 0 | 41 | L | G | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,642 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.662336 | 0.057033 | 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":12121966,"numValue":-0.662336458738464,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121967,"numValue":0.0570327442252667,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20149 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,149 | train | mutant | 476,591 | 358 | 477,943 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41M | L41M | 1 | 1 | 0 | 0 | 41 | L | M | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,231 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.065562 | 1.288555 | 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":2366576,"numValue":2.065562123682942,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366577,"numValue":1.2885549116704018,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366578,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20150 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,150 | train | mutant | 476,591 | 358 | 477,943 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41M | L41M | 1 | 1 | 0 | 0 | 41 | L | M | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,165 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.153963 | 0.041397 | 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":12123012,"numValue":-0.153963039424953,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123013,"numValue":0.041397417908204,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,151 | train | mutant | 476,592 | 358 | 477,944 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41V | L41V | 1 | 1 | 0 | 0 | 41 | L | V | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,232 | MegaScale | null | null | null | null | 4.701903 | null | null | null | null | null | null | 2.068177 | 1.232604 | 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":2366579,"numValue":2.068176838662525,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366580,"numValue":1.2326040915768357,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366581,"numValue":4.7019028854781695,"references":[],"strValue":null,"ty... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20152 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,152 | train | mutant | 476,592 | 358 | 477,944 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41V | L41V | 1 | 1 | 0 | 0 | 41 | L | V | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,172 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.181382 | 0.033479 | 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":12123026,"numValue":-0.181381610659969,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123027,"numValue":0.033479171533852,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20153 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,153 | train | mutant | 476,593 | 358 | 477,945 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41I | L41I | 1 | 1 | 0 | 0 | 41 | L | I | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,233 | MegaScale | null | null | null | null | 4.956139 | null | null | null | null | null | null | 2.154307 | 1.346988 | 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":2366582,"numValue":2.154307071450164,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366583,"numValue":1.34698846576687,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366584,"numValue":4.956138942202652,"references":[],"strValue":null,"type"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,154 | train | mutant | 476,593 | 358 | 477,945 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41I | L41I | 1 | 1 | 0 | 0 | 41 | L | I | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,644 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.091312 | 0.093915 | 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":12121970,"numValue":-0.0913124352417729,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121971,"numValue":0.0939145099707046,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20155 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,155 | train | mutant | 476,594 | 358 | 477,946 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41W | L41W | 1 | 1 | 0 | 0 | 41 | L | W | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,234 | MegaScale | null | null | null | null | 3.187136 | null | null | null | null | null | null | 1.22517 | 0.196423 | 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":2366585,"numValue":1.225170450718089,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366586,"numValue":0.1964226461594627,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366587,"numValue":3.1871357877864543,"references":[],"strValue":null,"ty... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,156 | train | mutant | 476,594 | 358 | 477,946 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41W | L41W | 1 | 1 | 0 | 0 | 41 | L | W | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,173 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.51712 | 0.042569 | 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":12123028,"numValue":-0.517119724571641,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123029,"numValue":0.0425689648859142,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,157 | train | mutant | 476,595 | 358 | 477,947 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41Y | L41Y | 1 | 1 | 0 | 0 | 41 | L | Y | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,235 | MegaScale | null | null | null | null | 2.765994 | null | null | null | null | null | null | 0.916177 | 0.031846 | 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":2366588,"numValue":0.9161768005581228,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366589,"numValue":0.0318456885283885,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366590,"numValue":2.7659944031101573,"references":[],"strValue":null,"t... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20158 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,158 | train | mutant | 476,595 | 358 | 477,947 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41Y | L41Y | 1 | 1 | 0 | 0 | 41 | L | Y | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,065,174 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.477163 | 0.076515 | 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":12123030,"numValue":-0.477163242958914,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123031,"numValue":0.0765150059375317,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20159 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,159 | train | mutant | 476,596 | 358 | 477,948 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41F | L41F | 1 | 1 | 0 | 0 | 41 | L | F | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,236 | MegaScale | null | null | null | null | 4.085605 | null | null | null | null | null | null | 1.860792 | 0.78905 | 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":2366591,"numValue":1.860791519603635,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366592,"numValue":0.7890503185524415,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366593,"numValue":4.085605268465697,"references":[],"strValue":null,"typ... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,160 | train | mutant | 476,596 | 358 | 477,948 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41F | L41F | 1 | 1 | 0 | 0 | 41 | L | F | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,641 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.342824 | 0.052524 | 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":12121964,"numValue":-0.342824449566187,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121965,"numValue":0.0525239002440702,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,161 | train | mutant | 476,597 | 358 | 477,949 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41P | L41P | 1 | 1 | 0 | 0 | 41 | L | P | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,237 | MegaScale | null | null | null | null | 2.237863 | null | null | null | null | null | null | 0.661036 | -0.513413 | 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":2366594,"numValue":0.6610363902056325,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366595,"numValue":-0.5134131338853059,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366596,"numValue":2.2378631280961043,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,163 | train | mutant | 476,598 | 358 | 477,950 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41C | L41C | 1 | 1 | 0 | 0 | 41 | L | C | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,238 | MegaScale | null | null | null | null | 4.025879 | null | null | null | null | null | null | 1.757797 | 0.701273 | 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":2366597,"numValue":1.757796985359663,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366598,"numValue":0.7012728396146294,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366599,"numValue":4.02587886800605,"references":[],"strValue":null,"type... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20164 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,164 | train | mutant | 476,598 | 358 | 477,950 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | L41C | L41C | 1 | 1 | 0 | 0 | 41 | L | C | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 5,064,638 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.361257 | 0.05926 | 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":12121958,"numValue":-0.361257447828629,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121959,"numValue":0.0592603873683575,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,166 | train | mutant | 476,600 | 358 | 477,952 | 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 | insA41 | insA41 | 1 | 0 | 0 | 1 | 41 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,240 | MegaScale | null | null | null | null | 3.899251 | null | null | null | null | null | null | 1.49298 | 0.677968 | 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":2366603,"numValue":1.492979675579938,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366604,"numValue":0.6779680770177933,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366605,"numValue":3.899251149244596,"references":[],"strValue":null,"typ... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20167 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,167 | train | mutant | 476,601 | 358 | 477,953 | 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 | delL41 | delL41 | 1 | 0 | 1 | 0 | 41 | L | - | 9 | CONSERVATION | 1CSP | 247 | null | 41 | A | L | false | false | 6.753738 | 24.76125 | 502,241 | MegaScale | null | null | null | null | 2.083116 | null | null | null | null | null | null | 0.519633 | -0.567202 | 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":2366606,"numValue":0.5196333018507688,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366607,"numValue":-0.5672022162800874,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366608,"numValue":2.0831155069376166,"references":[],"strValue":null,"... | [{"id":20849,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,169 | train | mutant | 1,156 | 358 | 1,302 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E42Q | E42Q | 1 | 1 | 0 | 0 | 42 | E | Q | 1 | CONSERVATION | 1CSP | 247 | null | 42 | A | L | false | false | 123.85509 | 41.135555 | 2,065 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E42Q | 50.5 | null | null | null | 33.94 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E42Q","t... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7743,"numValue":50.... | [{"id":20850,"numValue":1.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20170 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,170 | train | mutant | 1,156 | 358 | 1,302 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E42Q | E42Q | 1 | 1 | 0 | 0 | 42 | E | Q | 1 | CONSERVATION | 1CSP | 247 | null | 42 | A | L | false | false | 123.85509 | 41.135555 | 2,097 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E42Q | 53 | null | null | null | null | null | 34.66 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E42Q","ty... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7839,"numValue":53.0,"references":[],"strValue":null,"typ... | [{"id":20850,"numValue":1.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,171 | train | mutant | 1,156 | 358 | 1,302 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E42Q | E42Q | 1 | 1 | 0 | 0 | 42 | E | Q | 1 | CONSERVATION | 1CSP | 247 | null | 42 | A | L | false | false | 123.85509 | 41.135555 | 2,142 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E42Q | 54.1 | null | null | null | null | null | 35.61 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":7974,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7975,"numValue":35.61,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":7976,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20850,"numValue":1.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20172 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,172 | train | mutant | 1,156 | 358 | 1,302 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E42Q | E42Q | 1 | 1 | 0 | 0 | 42 | E | Q | 1 | CONSERVATION | 1CSP | 247 | null | 42 | A | L | false | false | 123.85509 | 41.135555 | 2,188 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E42Q | 54.7 | null | null | null | null | null | 36.09 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8112,"numValue":54.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8113,"numValue":36.09,"references":[],"strValue":null,"type... | [{"id":20850,"numValue":1.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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