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:19188 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,188 | train | mutant | 476,303 | 358 | 477,655 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H | V28H | 1 | 1 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,527 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.534259 | 0.126509 | 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":12121736,"numValue":-0.53425898433094,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121737,"numValue":0.126509323252645,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19189 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,189 | train | mutant | 476,304 | 358 | 477,656 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28D | V28D | 1 | 1 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,938 | MegaScale | null | null | null | null | 0.272512 | null | null | null | null | null | null | -0.486136 | -1.409416 | 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":2365698,"numValue":-0.4861360589409418,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365699,"numValue":-1.4094163469428715,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365700,"numValue":0.2725121170168534,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19190 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,190 | train | mutant | 476,304 | 358 | 477,656 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28D | V28D | 1 | 1 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,581 | MegaScale | null | null | null | null | 0.299513 | null | null | null | null | null | null | -0.576063 | -1.427798 | 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":3526137,"numValue":-0.5760625171214826,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526138,"numValue":-1.427797692643875,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526139,"numValue":0.2995126005726649,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19192 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,192 | train | mutant | 476,305 | 358 | 477,657 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28R | V28R | 1 | 1 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,939 | MegaScale | null | null | null | null | 0.243717 | null | null | null | null | null | null | -0.744851 | -1.882611 | 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":2365701,"numValue":-0.7448513197077167,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365702,"numValue":-1.882611343285867,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365703,"numValue":0.2437172321248907,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19193 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,193 | train | mutant | 476,305 | 358 | 477,657 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28R | V28R | 1 | 1 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,601 | MegaScale | null | null | null | null | 0.203412 | null | null | null | null | null | null | -0.682766 | -1.878549 | 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":3526197,"numValue":-0.6827659053134815,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526198,"numValue":-1.8785488919315136,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526199,"numValue":0.2034121503161531,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19194 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,194 | train | mutant | 476,305 | 358 | 477,657 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28R | V28R | 1 | 1 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,535 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.742684 | 0.056193 | 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":12121752,"numValue":-0.742683673545118,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121753,"numValue":0.056193166634292,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19195 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,195 | train | mutant | 476,306 | 358 | 477,658 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28K | V28K | 1 | 1 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,940 | MegaScale | null | null | null | null | 0.283559 | null | null | null | null | null | null | -0.564145 | -1.803406 | 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":2365704,"numValue":-0.5641447541457258,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365705,"numValue":-1.803405960385308,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365706,"numValue":0.2835593787700639,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19196 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,196 | train | mutant | 476,306 | 358 | 477,658 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28K | V28K | 1 | 1 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,621 | MegaScale | null | null | null | null | 0.379346 | null | null | null | null | null | null | -0.516373 | -1.681952 | 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":3526257,"numValue":-0.5163729379848481,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526258,"numValue":-1.6819518948812182,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526259,"numValue":0.3793462897969547,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19197 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,197 | train | mutant | 476,306 | 358 | 477,658 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28K | V28K | 1 | 1 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,529 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.8126 | 0.084644 | 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":12121740,"numValue":-0.812600202172325,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121741,"numValue":0.0846436680568646,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19198 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,198 | train | mutant | 476,307 | 358 | 477,659 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28T | V28T | 1 | 1 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,941 | MegaScale | null | null | null | null | 4.18892 | null | null | null | null | null | null | 1.953337 | 0.841376 | 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":2365707,"numValue":1.9533368734799528,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365708,"numValue":0.841375646260095,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365709,"numValue":4.188920204426332,"references":[],"strValue":null,"typ... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19199 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,199 | train | mutant | 476,307 | 358 | 477,659 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28T | V28T | 1 | 1 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,641 | MegaScale | null | null | null | null | 3.996413 | null | null | null | null | null | null | 1.641265 | 0.696291 | 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":3526317,"numValue":1.641264789952594,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526318,"numValue":0.6962910743103629,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526319,"numValue":3.996412715615863,"references":[],"strValue":null,"typ... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19200 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,200 | train | mutant | 476,307 | 358 | 477,659 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28T | V28T | 1 | 1 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,537 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.296591 | 0.04459 | 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":12121756,"numValue":-0.296590763211261,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121757,"numValue":0.0445896699767718,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19201 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,201 | train | mutant | 476,308 | 358 | 477,660 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28S | V28S | 1 | 1 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,942 | MegaScale | null | null | null | null | 2.222851 | null | null | null | null | null | null | 0.845279 | -0.543224 | 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":2365710,"numValue":0.845278787781466,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365711,"numValue":-0.5432238178200075,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365712,"numValue":2.222851257702201,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19202 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,202 | train | mutant | 476,308 | 358 | 477,660 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28S | V28S | 1 | 1 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,661 | MegaScale | null | null | null | null | 2.435701 | null | null | null | null | null | null | 0.773558 | -0.366159 | 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":3526377,"numValue":0.7735580222699169,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526378,"numValue":-0.3661593620018457,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526379,"numValue":2.435700650784126,"references":[],"strValue":null,"t... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19203 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,203 | train | mutant | 476,308 | 358 | 477,660 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28S | V28S | 1 | 1 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,536 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.801116 | 0.062335 | 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":12121754,"numValue":-0.801115842558777,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121755,"numValue":0.062335342442026,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19204 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,204 | train | mutant | 476,309 | 358 | 477,661 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A | V28A | 1 | 1 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,943 | MegaScale | null | null | null | null | 3.917429 | null | null | null | null | null | null | 1.694294 | 0.752105 | 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":2365713,"numValue":1.6942938334452902,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365714,"numValue":0.7521045854795321,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365715,"numValue":3.917428675332169,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19205 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,205 | train | mutant | 476,309 | 358 | 477,661 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A | V28A | 1 | 1 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,681 | MegaScale | null | null | null | null | 3.829975 | null | null | null | null | null | null | 1.679855 | 0.547944 | 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":3526437,"numValue":1.6798546542195432,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526438,"numValue":0.547944111993904,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526439,"numValue":3.8299749967761434,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19206 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,206 | train | mutant | 476,309 | 358 | 477,661 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A | V28A | 1 | 1 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,521 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.310804 | 0.035688 | 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":12121724,"numValue":-0.310803915599893,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121725,"numValue":0.0356881259118593,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19207 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,207 | train | mutant | 476,310 | 358 | 477,662 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G | V28G | 1 | 1 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,944 | MegaScale | null | null | null | null | 1.044765 | null | null | null | null | null | null | -0.055237 | -1.195007 | 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":2365716,"numValue":-0.0552371180361552,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365717,"numValue":-1.1950068007795704,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365718,"numValue":1.0447645384010555,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19208 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,208 | train | mutant | 476,310 | 358 | 477,662 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G | V28G | 1 | 1 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,701 | MegaScale | null | null | null | null | 1.142777 | null | null | null | null | null | null | -0.114731 | -1.125242 | 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":3526497,"numValue":-0.1147312325526105,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526498,"numValue":-1.1252416702971937,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526499,"numValue":1.1427769503216365,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19209 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,209 | train | mutant | 476,310 | 358 | 477,662 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G | V28G | 1 | 1 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,526 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.893647 | 0.051765 | 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":12121734,"numValue":-0.893646819631582,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121735,"numValue":0.0517650333389291,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19210 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,210 | train | mutant | 476,311 | 358 | 477,663 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M | V28M | 1 | 1 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,945 | MegaScale | null | null | null | null | 4.506291 | null | null | null | null | null | null | 2.065601 | 1.086375 | 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":2365719,"numValue":2.065601281948328,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365720,"numValue":1.0863752837644276,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365721,"numValue":4.506290658825584,"references":[],"strValue":null,"typ... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19211 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,211 | train | mutant | 476,311 | 358 | 477,663 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M | V28M | 1 | 1 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,721 | MegaScale | null | null | null | null | 4.310652 | null | null | null | null | null | null | 1.876781 | 0.855895 | 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":3526557,"numValue":1.8767814315158329,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526558,"numValue":0.85589544846202,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526559,"numValue":4.310652180879244,"references":[],"strValue":null,"type... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19212 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,212 | train | mutant | 476,311 | 358 | 477,663 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M | V28M | 1 | 1 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,531 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.167175 | 0.048102 | 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":12121744,"numValue":-0.167175205117937,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121745,"numValue":0.0481021887199717,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19213 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,213 | train | mutant | 476,312 | 358 | 477,664 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L | V28L | 1 | 1 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,946 | MegaScale | null | null | null | null | 4.849283 | null | null | null | null | null | null | 2.152324 | 1.338971 | 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":2365722,"numValue":2.152324067419705,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365723,"numValue":1.3389709595861086,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365724,"numValue":4.849282818683602,"references":[],"strValue":null,"typ... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19215 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,215 | train | mutant | 476,312 | 358 | 477,664 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L | V28L | 1 | 1 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,530 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.201166 | 0.027503 | 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":12121742,"numValue":-0.201166431641288,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121743,"numValue":0.0275033974972757,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19216 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,216 | train | mutant | 476,313 | 358 | 477,665 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28I | V28I | 1 | 1 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,947 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.535029 | 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":2365725,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365726,"numValue":1.535028667989924,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365727,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19217 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,217 | train | mutant | 476,313 | 358 | 477,665 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28I | V28I | 1 | 1 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,800 | MegaScale | null | null | null | null | 4.574704 | null | null | null | null | null | null | 1.931597 | 1.07409 | 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":3526794,"numValue":1.931597039127244,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526795,"numValue":1.07409029200329,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526796,"numValue":4.574703571670828,"references":[],"strValue":null,"type"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19218 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,218 | train | mutant | 476,313 | 358 | 477,665 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28I | V28I | 1 | 1 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,528 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.176256 | 0.052313 | 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":12121738,"numValue":-0.17625584729261,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121739,"numValue":0.0523127668799508,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19219 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,219 | train | mutant | 476,314 | 358 | 477,666 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W | V28W | 1 | 1 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,948 | MegaScale | null | null | null | null | 2.450246 | null | null | null | null | null | null | 0.799624 | -0.508168 | 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":2365728,"numValue":0.7996244148921279,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365729,"numValue":-0.5081677936156435,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365730,"numValue":2.4502456147765623,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19220 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,220 | train | mutant | 476,314 | 358 | 477,666 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W | V28W | 1 | 1 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,820 | MegaScale | null | null | null | null | 2.654983 | null | null | null | null | null | null | 0.716713 | -0.270939 | 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":3526854,"numValue":0.7167129956056338,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526855,"numValue":-0.2709386592241962,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526856,"numValue":2.654983108419267,"references":[],"strValue":null,"t... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19221 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,221 | train | mutant | 476,314 | 358 | 477,666 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W | V28W | 1 | 1 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,065,317 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.950519 | 0.088389 | 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":12123316,"numValue":-0.950518995041252,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123317,"numValue":0.0883889039398088,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19222 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,222 | train | mutant | 476,315 | 358 | 477,667 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y | V28Y | 1 | 1 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,949 | MegaScale | null | null | null | null | 3.40345 | null | null | null | null | null | null | 1.323679 | 0.454983 | 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":2365731,"numValue":1.3236793610180198,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365732,"numValue":0.4549826855375105,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365733,"numValue":3.403449903853611,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19223 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,223 | train | mutant | 476,315 | 358 | 477,667 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y | V28Y | 1 | 1 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,840 | MegaScale | null | null | null | null | 3.485579 | null | null | null | null | null | null | 1.290979 | 0.401174 | 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":3526914,"numValue":1.2909793636241362,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526915,"numValue":0.4011740435576784,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526916,"numValue":3.485578952228892,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19224 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,224 | train | mutant | 476,315 | 358 | 477,667 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y | V28Y | 1 | 1 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,065,318 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.414565 | 0.071469 | 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":12123318,"numValue":-0.414564896169404,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123319,"numValue":0.0714687326901217,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19225 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,225 | train | mutant | 476,316 | 358 | 477,668 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F | V28F | 1 | 1 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,950 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.23478 | 1.723573 | 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":2365734,"numValue":2.234780259211436,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365735,"numValue":1.7235727840086754,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365736,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19226 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,226 | train | mutant | 476,316 | 358 | 477,668 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F | V28F | 1 | 1 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,860 | MegaScale | null | null | null | null | 4.620578 | null | null | null | null | null | null | 1.968212 | 1.062809 | 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":3526974,"numValue":1.9682124740187712,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526975,"numValue":1.0628092137756333,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526976,"numValue":4.6205777370027725,"references":[],"strValue":null,"t... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,228 | train | mutant | 476,317 | 358 | 477,669 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P | V28P | 1 | 1 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,951 | MegaScale | null | null | null | null | -0.062562 | null | null | null | null | null | null | -0.548479 | -1.416961 | 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":2365737,"numValue":-0.5484789447094902,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365738,"numValue":-1.4169609579979787,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365739,"numValue":-0.0625616922966817,"references":[],"strValue":null... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,229 | train | mutant | 476,317 | 358 | 477,669 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P | V28P | 1 | 1 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,880 | MegaScale | null | null | null | null | 0.19429 | null | null | null | null | null | null | -0.699829 | -1.329113 | 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":3527034,"numValue":-0.6998290718145121,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527035,"numValue":-1.3291126799349366,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527036,"numValue":0.1942901191809202,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19230 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,230 | train | mutant | 476,317 | 358 | 477,669 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P | V28P | 1 | 1 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,533 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.867842 | 0.071812 | 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":12121748,"numValue":-0.867842339443298,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121749,"numValue":0.0718123311869979,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,231 | train | mutant | 476,318 | 358 | 477,670 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C | V28C | 1 | 1 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,952 | MegaScale | null | null | null | null | 4.599917 | null | null | null | null | null | null | 2.05522 | 1.042548 | 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":2365740,"numValue":2.0552197282446905,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365741,"numValue":1.0425478245057218,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365742,"numValue":4.599917446107794,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19232 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,232 | train | mutant | 476,318 | 358 | 477,670 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C | V28C | 1 | 1 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 778,741 | MegaScale | null | null | null | null | 4.580898 | null | null | null | null | null | null | 1.948594 | 1.05089 | 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":3526617,"numValue":1.948593878712842,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526618,"numValue":1.0508903396764353,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526619,"numValue":4.58089809881978,"references":[],"strValue":null,"type... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19233 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,233 | train | mutant | 476,318 | 358 | 477,670 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C | V28C | 1 | 1 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,522 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.046366 | 0.083843 | 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":12121726,"numValue":0.0463655565384826,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121727,"numValue":0.0838428787003464,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,235 | train | mutant | 476,320 | 358 | 477,672 | 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 | insA28 | insA28 | 1 | 0 | 0 | 1 | 28 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 501,954 | MegaScale | null | null | null | null | 1.932891 | null | null | null | null | null | null | 0.432971 | -0.73657 | 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":2365746,"numValue":0.4329705442909435,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365747,"numValue":-0.7365699494475039,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365748,"numValue":1.9328905553362208,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19237 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,237 | train | mutant | 476,321 | 358 | 477,673 | 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 | delV28 | delV28 | 1 | 0 | 1 | 0 | 28 | V | - | 9 | CONSERVATION | 1CSP | 247 | null | 28 | A | E | false | false | 0 | 12.77 | 5,064,520 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.968204 | 0.084948 | 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":12121722,"numValue":-0.968203522675814,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121723,"numValue":0.0849483801833339,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,238 | train | mutant | 727,694 | 358 | 727,885 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63Q | V28Q|V63Q | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,487 | MegaScale | null | null | null | null | 0.322443 | null | null | null | null | null | null | -0.65535 | -1.675315 | 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":3525855,"numValue":-0.655349611355255,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525856,"numValue":-1.675314953097491,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525857,"numValue":0.3224428407002107,"references":[],"strValue":null,"t... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,239 | train | mutant | 727,695 | 358 | 727,886 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63E | V28Q|V63E | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,488 | MegaScale | null | null | null | null | 0.480971 | null | null | null | null | null | null | -0.592992 | -1.547788 | 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":3525858,"numValue":-0.5929923824169787,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525859,"numValue":-1.5477882412151205,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525860,"numValue":0.4809712616550994,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19240 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,240 | train | mutant | 727,696 | 358 | 727,887 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63N | V28Q|V63N | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,489 | MegaScale | null | null | null | null | 0.394436 | null | null | null | null | null | null | -0.623691 | -1.628745 | 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":3525861,"numValue":-0.6236910928373096,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525862,"numValue":-1.628745004486622,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525863,"numValue":0.3944361315889164,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19241 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,241 | train | mutant | 727,697 | 358 | 727,888 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63H | V28Q|V63H | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,490 | MegaScale | null | null | null | null | 0.168919 | null | null | null | null | null | null | -0.649849 | -1.713371 | 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":3525864,"numValue":-0.6498485124284086,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525865,"numValue":-1.71337089428242,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525866,"numValue":0.168919422168552,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19242 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,242 | train | mutant | 727,698 | 358 | 727,889 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63D | V28Q|V63D | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,491 | MegaScale | null | null | null | null | 0.326499 | null | null | null | null | null | null | -0.569564 | -1.660053 | 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":3525867,"numValue":-0.5695643972841857,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525868,"numValue":-1.6600527865281156,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525869,"numValue":0.3264985418929703,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,243 | train | mutant | 727,699 | 358 | 727,890 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63R | V28Q|V63R | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,492 | MegaScale | null | null | null | null | 0.303649 | null | null | null | null | null | null | -0.864943 | -1.696125 | 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":3525870,"numValue":-0.8649428560302894,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525871,"numValue":-1.696124823326487,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525872,"numValue":0.3036494332601506,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19244 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,244 | train | mutant | 727,700 | 358 | 727,891 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63K | V28Q|V63K | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,493 | MegaScale | null | null | null | null | 0.567686 | null | null | null | null | null | null | -0.575731 | -1.563375 | 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":3525873,"numValue":-0.5757311869005053,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525874,"numValue":-1.563375012866036,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525875,"numValue":0.5676860716995397,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19246 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,246 | train | mutant | 727,702 | 358 | 727,893 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63S | V28Q|V63S | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,495 | MegaScale | null | null | null | null | 0.309633 | null | null | null | null | null | null | -0.64472 | -1.700398 | 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":3525879,"numValue":-0.6447201517736256,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525880,"numValue":-1.700398067152261,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525881,"numValue":0.3096334438276668,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19247 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,247 | train | mutant | 727,703 | 358 | 727,894 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63A | V28Q|V63A | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,496 | MegaScale | null | null | null | null | 0.243912 | null | null | null | null | null | null | -0.720407 | -1.686704 | 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":3525882,"numValue":-0.7204072910081964,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525883,"numValue":-1.6867039576773206,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525884,"numValue":0.2439121691992689,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19248 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,248 | train | mutant | 727,704 | 358 | 727,895 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Q|V63G | V28Q|V63G | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,497 | MegaScale | null | null | null | null | 0.233544 | null | null | null | null | null | null | -0.577406 | -1.721557 | 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":3525885,"numValue":-0.5774055844776911,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525886,"numValue":-1.7215571208991256,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525887,"numValue":0.2335438186968064,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,249 | train | mutant | 727,705 | 358 | 727,896 | 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 | V28Q|V63M | V28Q|V63M | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,498 | MegaScale | null | null | null | null | 0.549081 | null | null | null | null | null | null | -0.568607 | -1.680233 | 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":3525888,"numValue":-0.5686067984051777,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525889,"numValue":-1.680232535307827,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525890,"numValue":0.5490811501196797,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,250 | train | mutant | 727,706 | 358 | 727,897 | 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 | V28Q|V63C | V28Q|V63C | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,499 | MegaScale | null | null | null | null | 0.629 | null | null | null | null | null | null | -0.560101 | -1.588044 | 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":3525891,"numValue":-0.5601013642038326,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525892,"numValue":-1.588043624311429,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525893,"numValue":0.6290003541147833,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,251 | train | mutant | 727,707 | 358 | 727,898 | 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 | V28Q|V63L | V28Q|V63L | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,500 | MegaScale | null | null | null | null | 0.362085 | null | null | null | null | null | null | -0.720084 | -1.705485 | 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":3525894,"numValue":-0.7200844026595554,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525895,"numValue":-1.7054849501950478,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525896,"numValue":0.3620849997806939,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,252 | train | mutant | 727,708 | 358 | 727,899 | 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 | V28Q|V63I | V28Q|V63I | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,502 | MegaScale | null | null | null | null | 0.725711 | null | null | null | null | null | null | -0.490053 | -1.465234 | 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":3525900,"numValue":-0.4900528544708189,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525901,"numValue":-1.465233921829903,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525902,"numValue":0.7257114853045405,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19253 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,253 | train | mutant | 727,709 | 358 | 727,900 | 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 | V28Q|V63W | V28Q|V63W | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,503 | MegaScale | null | null | null | null | 0.342897 | null | null | null | null | null | null | -0.727447 | -1.865093 | 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":3525903,"numValue":-0.7274466053678399,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525904,"numValue":-1.865093170905064,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525905,"numValue":0.3428968510032698,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19254 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,254 | train | mutant | 727,710 | 358 | 727,901 | 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 | V28Q|V63Y | V28Q|V63Y | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,504 | MegaScale | null | null | null | null | 0.395776 | null | null | null | null | null | null | -0.597322 | -1.927227 | 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":3525906,"numValue":-0.5973216532243306,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525907,"numValue":-1.9272269905524868,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525908,"numValue":0.3957759637718229,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,255 | train | mutant | 727,711 | 358 | 727,902 | 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 | V28Q|V63F | V28Q|V63F | 2 | 2 | 0 | 0 | 28 | V | Q | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,505 | MegaScale | null | null | null | null | 0.135645 | null | null | null | null | null | null | -0.624162 | -1.987609 | 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":3525909,"numValue":-0.6241619916236791,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525910,"numValue":-1.987609109976584,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525911,"numValue":0.1356453683940365,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,258 | train | mutant | 727,714 | 358 | 727,905 | 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 | V28E|V63E | V28E|V63E | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,508 | MegaScale | null | null | null | null | 0.27772 | null | null | null | null | null | null | -0.544909 | -1.479953 | 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":3525918,"numValue":-0.5449091023403541,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525919,"numValue":-1.479952908288806,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525920,"numValue":0.2777204729392069,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,259 | train | mutant | 727,715 | 358 | 727,906 | 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 | V28E|V63N | V28E|V63N | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,509 | MegaScale | null | null | null | null | 0.423955 | null | null | null | null | null | null | -0.461486 | -1.467154 | 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":3525921,"numValue":-0.4614856905548234,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525922,"numValue":-1.4671535501807629,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525923,"numValue":0.423954804336766,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,260 | train | mutant | 727,716 | 358 | 727,907 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E|V63H | V28E|V63H | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,510 | MegaScale | null | null | null | null | 0.301753 | null | null | null | null | null | null | -0.600619 | -1.464255 | 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":3525924,"numValue":-0.6006187950969035,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525925,"numValue":-1.4642553749656528,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525926,"numValue":0.3017527058497657,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,261 | train | mutant | 727,717 | 358 | 727,908 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E|V63D | V28E|V63D | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,511 | MegaScale | null | null | null | null | 0.330059 | null | null | null | null | null | null | -0.563923 | -1.43373 | 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":3525927,"numValue":-0.5639233522621275,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525928,"numValue":-1.4337295810921429,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525929,"numValue":0.3300594949238764,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,262 | train | mutant | 727,718 | 358 | 727,909 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E|V63R | V28E|V63R | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,512 | MegaScale | null | null | null | null | 0.236652 | null | null | null | null | null | null | -0.874043 | -1.503371 | 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":3525930,"numValue":-0.874043422551653,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525931,"numValue":-1.5033708883751205,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525932,"numValue":0.2366516215314965,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,264 | train | mutant | 727,720 | 358 | 727,911 | 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 | V28E|V63T | V28E|V63T | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,514 | MegaScale | null | null | null | null | 0.278413 | null | null | null | null | null | null | -0.686572 | -1.465674 | 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":3525936,"numValue":-0.6865721706685188,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525937,"numValue":-1.465673848028909,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525938,"numValue":0.2784125678126943,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,265 | train | mutant | 727,721 | 358 | 727,912 | 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 | V28E|V63S | V28E|V63S | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,515 | MegaScale | null | null | null | null | 0.131903 | null | null | null | null | null | null | -0.602794 | -1.478066 | 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":3525939,"numValue":-0.6027941828351314,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525940,"numValue":-1.4780658605634387,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525941,"numValue":0.1319032469922845,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,266 | train | mutant | 727,722 | 358 | 727,913 | 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 | V28E|V63A | V28E|V63A | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,516 | MegaScale | null | null | null | null | 0.358858 | null | null | null | null | null | null | -0.643529 | -1.440748 | 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":3525942,"numValue":-0.6435289578561425,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525943,"numValue":-1.4407478468469508,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525944,"numValue":0.3588580139838149,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19267 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,267 | train | mutant | 727,723 | 358 | 727,914 | 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 | V28E|V63G | V28E|V63G | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,517 | MegaScale | null | null | null | null | 0.315093 | null | null | null | null | null | null | -0.529275 | -1.484033 | 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":3525945,"numValue":-0.5292752488844794,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525946,"numValue":-1.4840329091039717,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525947,"numValue":0.3150930208827566,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,268 | train | mutant | 727,724 | 358 | 727,915 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28E|V63M | V28E|V63M | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,518 | MegaScale | null | null | null | null | 0.164705 | null | null | null | null | null | null | -0.703746 | -1.590175 | 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":3525948,"numValue":-0.7037459772342434,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525949,"numValue":-1.5901747686001944,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525950,"numValue":0.1647045686209587,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,269 | train | mutant | 727,725 | 358 | 727,916 | 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 | V28E|V63C | V28E|V63C | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,519 | MegaScale | null | null | null | null | 0.557254 | null | null | null | null | null | null | -0.531871 | -1.321933 | 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":3525951,"numValue":-0.5318713224042761,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525952,"numValue":-1.321933227160743,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525953,"numValue":0.5572542487948942,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19270 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,270 | train | mutant | 727,726 | 358 | 727,917 | 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 | V28E|V63L | V28E|V63L | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,520 | MegaScale | null | null | null | null | 0.612776 | null | null | null | null | null | null | -0.547057 | -1.46866 | 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":3525954,"numValue":-0.5470574374453818,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525955,"numValue":-1.4686601339044325,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525956,"numValue":0.6127756834911358,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,271 | train | mutant | 727,727 | 358 | 727,918 | 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 | V28E|V63I | V28E|V63I | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,522 | MegaScale | null | null | null | null | 0.526514 | null | null | null | null | null | null | -0.548496 | -1.351112 | 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":3525960,"numValue":-0.5484961113890249,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525961,"numValue":-1.3511122459408351,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525962,"numValue":0.526514174776421,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,272 | train | mutant | 727,728 | 358 | 727,919 | 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 | V28E|V63W | V28E|V63W | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,523 | MegaScale | null | null | null | null | -0.391039 | null | null | null | null | null | null | -0.85957 | -2.016162 | 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":3525963,"numValue":-0.8595704643377422,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525964,"numValue":-2.016162324978596,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525965,"numValue":-0.3910387730871256,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,273 | train | mutant | 727,729 | 358 | 727,920 | 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 | V28E|V63Y | V28E|V63Y | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,524 | MegaScale | null | null | null | null | -0.07146 | null | null | null | null | null | null | -0.756309 | -1.979656 | 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":3525966,"numValue":-0.7563090385196571,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525967,"numValue":-1.979656285036794,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525968,"numValue":-0.0714601661340437,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,274 | train | mutant | 727,730 | 358 | 727,921 | 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 | V28E|V63F | V28E|V63F | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,525 | MegaScale | null | null | null | null | 0.02811 | null | null | null | null | null | null | -0.764625 | -1.882366 | 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":3525969,"numValue":-0.7646250968998834,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525970,"numValue":-1.8823660660588584,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525971,"numValue":0.0281097450594075,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,275 | train | mutant | 727,731 | 358 | 727,922 | 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 | V28E|V63P | V28E|V63P | 2 | 2 | 0 | 0 | 28 | V | E | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,526 | MegaScale | null | null | null | null | 0.36969 | null | null | null | null | null | null | -0.447218 | -1.406036 | 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":3525972,"numValue":-0.4472184403785776,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525973,"numValue":-1.4060364009858155,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525974,"numValue":0.3696898692065935,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,276 | train | mutant | 727,732 | 358 | 727,923 | 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 | V28N|V63Q | V28N|V63Q | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,527 | MegaScale | null | null | null | null | 0.242204 | null | null | null | null | null | null | -0.616525 | -1.640673 | 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":3525975,"numValue":-0.6165246573786775,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525976,"numValue":-1.640672646872206,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525977,"numValue":0.2422035258237837,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,277 | train | mutant | 727,733 | 358 | 727,924 | 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 | V28N|V63E | V28N|V63E | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,528 | MegaScale | null | null | null | null | 0.400114 | null | null | null | null | null | null | -0.536747 | -1.52892 | 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":3525978,"numValue":-0.536747175546861,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525979,"numValue":-1.5289197729090511,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525980,"numValue":0.4001143750497113,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19278 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,278 | train | mutant | 727,734 | 358 | 727,925 | 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 | V28N|V63N | V28N|V63N | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,529 | MegaScale | null | null | null | null | 0.4376 | null | null | null | null | null | null | -0.592829 | -1.528448 | 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":3525981,"numValue":-0.5928289323684106,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525982,"numValue":-1.528448395490385,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525983,"numValue":0.437600388068855,"references":[],"strValue":null,"t... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,279 | train | mutant | 727,735 | 358 | 727,926 | 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 | V28N|V63H | V28N|V63H | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,530 | MegaScale | null | null | null | null | 0.269444 | null | null | null | null | null | null | -0.704575 | -1.615741 | 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":3525984,"numValue":-0.7045752014332012,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525985,"numValue":-1.615741484062266,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525986,"numValue":0.2694435863512036,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,281 | train | mutant | 727,737 | 358 | 727,928 | 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 | V28N|V63R | V28N|V63R | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,532 | MegaScale | null | null | null | null | 0.333857 | null | null | null | null | null | null | -0.821196 | -1.666759 | 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":3525990,"numValue":-0.821195801517923,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525991,"numValue":-1.6667588627431629,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525992,"numValue":0.3338573371575785,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,282 | train | mutant | 727,738 | 358 | 727,929 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28N|V63K | V28N|V63K | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,533 | MegaScale | null | null | null | null | 0.528093 | null | null | null | null | null | null | -0.554039 | -1.554715 | 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":3525993,"numValue":-0.5540392080613976,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525994,"numValue":-1.5547145107960227,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525995,"numValue":0.5280932155017551,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,283 | train | mutant | 727,739 | 358 | 727,930 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28N|V63T | V28N|V63T | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,534 | MegaScale | null | null | null | null | 0.289658 | null | null | null | null | null | null | -0.572544 | -1.610063 | 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":3525996,"numValue":-0.5725444153879227,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3525997,"numValue":-1.6100627917226733,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3525998,"numValue":0.2896584900375464,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,284 | train | mutant | 727,740 | 358 | 727,931 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28N|V63S | V28N|V63S | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,535 | MegaScale | null | null | null | null | 0.211418 | null | null | null | null | null | null | -0.566273 | -1.603539 | 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":3525999,"numValue":-0.5662726251616377,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526000,"numValue":-1.6035385146584888,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526001,"numValue":0.211417667405969,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,285 | train | mutant | 727,741 | 358 | 727,932 | 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 | V28N|V63A | V28N|V63A | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,536 | MegaScale | null | null | null | null | 0.416521 | null | null | null | null | null | null | -0.654579 | -1.533947 | 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":3526002,"numValue":-0.6545790148466415,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526003,"numValue":-1.5339465435005444,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526004,"numValue":0.4165209751950386,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,286 | train | mutant | 727,742 | 358 | 727,933 | 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 | V28N|V63G | V28N|V63G | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,537 | MegaScale | null | null | null | null | 0.539837 | null | null | null | null | null | null | -0.523804 | -1.602999 | 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":3526005,"numValue":-0.5238042106179644,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526006,"numValue":-1.6029994890227155,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526007,"numValue":0.5398367515586164,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,287 | train | mutant | 727,743 | 358 | 727,934 | 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 | V28N|V63M | V28N|V63M | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,538 | MegaScale | null | null | null | null | 0.458471 | null | null | null | null | null | null | -0.744336 | -1.551152 | 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":3526008,"numValue":-0.7443364119572893,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526009,"numValue":-1.5511524050651582,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526010,"numValue":0.4584713291068132,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,288 | train | mutant | 727,744 | 358 | 727,935 | 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 | V28N|V63C | V28N|V63C | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,539 | MegaScale | null | null | null | null | 0.423318 | null | null | null | null | null | null | -0.437436 | -1.60272 | 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":3526011,"numValue":-0.4374362737689283,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526012,"numValue":-1.6027204731393638,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526013,"numValue":0.4233177711158718,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,289 | train | mutant | 727,745 | 358 | 727,936 | 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 | V28N|V63L | V28N|V63L | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,540 | MegaScale | null | null | null | null | 0.463854 | null | null | null | null | null | null | -0.672865 | -1.542562 | 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":3526014,"numValue":-0.6728651470147042,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526015,"numValue":-1.5425618834842931,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526016,"numValue":0.4638538734127746,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,290 | train | mutant | 727,746 | 358 | 727,937 | 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 | V28N|V63I | V28N|V63I | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,542 | MegaScale | null | null | null | null | 0.500421 | null | null | null | null | null | null | -0.477669 | -1.527442 | 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":3526020,"numValue":-0.4776685079958008,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526021,"numValue":-1.5274419047787369,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526022,"numValue":0.5004214958056664,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,291 | train | mutant | 727,747 | 358 | 727,938 | 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 | V28N|V63W | V28N|V63W | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,543 | MegaScale | null | null | null | null | 0.172893 | null | null | null | null | null | null | -0.670052 | -1.960969 | 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":3526023,"numValue":-0.6700519816621978,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526024,"numValue":-1.9609692644429824,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526025,"numValue":0.1728934397857043,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,292 | train | mutant | 727,748 | 358 | 727,939 | 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 | V28N|V63Y | V28N|V63Y | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,544 | MegaScale | null | null | null | null | -0.019095 | null | null | null | null | null | null | -0.652275 | -2.08043 | 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":3526026,"numValue":-0.6522750853324932,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526027,"numValue":-2.0804299373584536,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526028,"numValue":-0.0190954159990089,"references":[],"strValue":null... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,293 | train | mutant | 727,749 | 358 | 727,940 | 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 | V28N|V63F | V28N|V63F | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,545 | MegaScale | null | null | null | null | 0.175713 | null | null | null | null | null | null | -0.704846 | -1.898601 | 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":3526029,"numValue":-0.704846034920345,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526030,"numValue":-1.898601095885685,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526031,"numValue":0.175712663055527,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,294 | train | mutant | 727,750 | 358 | 727,941 | 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 | V28N|V63P | V28N|V63P | 2 | 2 | 0 | 0 | 28 | V | N | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,546 | MegaScale | null | null | null | null | 0.322428 | null | null | null | null | null | null | -0.590658 | -1.556579 | 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":3526032,"numValue":-0.590658297056246,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526033,"numValue":-1.5565785351285548,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526034,"numValue":0.3224284038504605,"references":[],"strValue":null,"... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,295 | train | mutant | 727,751 | 358 | 727,942 | 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 | V28H|V63Q | V28H|V63Q | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,547 | MegaScale | null | null | null | null | 0.363161 | null | null | null | null | null | null | -0.691318 | -1.548114 | 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":3526035,"numValue":-0.6913180524523401,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526036,"numValue":-1.548114452675754,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526037,"numValue":0.36316057348429,"references":[],"strValue":null,"ty... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,296 | train | mutant | 727,752 | 358 | 727,943 | 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 | V28H|V63E | V28H|V63E | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,548 | MegaScale | null | null | null | null | 0.533533 | null | null | null | null | null | null | -0.527269 | -1.469425 | 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":3526038,"numValue":-0.5272692585146177,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526039,"numValue":-1.469425006371712,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526040,"numValue":0.533533349621476,"references":[],"strValue":null,"t... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,297 | train | mutant | 727,753 | 358 | 727,944 | 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 | V28H|V63N | V28H|V63N | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,549 | MegaScale | null | null | null | null | 0.599677 | null | null | null | null | null | null | -0.398703 | -1.54303 | 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":3526041,"numValue":-0.3987031172232893,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526042,"numValue":-1.5430302096496045,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526043,"numValue":0.5996767782052781,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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