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:19298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,298 | train | mutant | 727,754 | 358 | 727,945 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H|V63H | V28H|V63H | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,550 | MegaScale | null | null | null | null | 0.383665 | null | null | null | null | null | null | -0.638277 | -1.587095 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526044,"numValue":-0.6382769535224058,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526045,"numValue":-1.587094588405482,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526046,"numValue":0.3836653426485349,"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:19299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,299 | train | mutant | 727,755 | 358 | 727,946 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H|V63D | V28H|V63D | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,551 | MegaScale | null | null | null | null | 0.486572 | null | null | null | null | null | null | -0.375161 | -1.546325 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526047,"numValue":-0.3751608939615286,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526048,"numValue":-1.5463246235020112,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526049,"numValue":0.4865724390712268,"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:19300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,300 | train | mutant | 727,756 | 358 | 727,947 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H|V63R | V28H|V63R | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,552 | MegaScale | null | null | null | null | 0.442587 | null | null | null | null | null | null | -0.799224 | -1.600265 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526050,"numValue":-0.799224246780702,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526051,"numValue":-1.6002649659603647,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526052,"numValue":0.442587335873523,"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:19301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,301 | train | mutant | 727,757 | 358 | 727,948 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H|V63K | V28H|V63K | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,553 | MegaScale | null | null | null | null | 0.528636 | null | null | null | null | null | null | -0.494565 | -1.495611 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526053,"numValue":-0.4945648048731377,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526054,"numValue":-1.4956114423532616,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526055,"numValue":0.5286360325178003,"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:19302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,302 | train | mutant | 727,758 | 358 | 727,949 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H|V63T | V28H|V63T | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,554 | MegaScale | null | null | null | null | 0.452937 | null | null | null | null | null | null | -0.586626 | -1.559165 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526056,"numValue":-0.5866262900291719,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526057,"numValue":-1.5591653058980983,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526058,"numValue":0.452937264952961,"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:19303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,303 | train | mutant | 727,759 | 358 | 727,950 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28H|V63S | V28H|V63S | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,555 | MegaScale | null | null | null | null | 0.446264 | null | null | null | null | null | null | -0.634763 | -1.528492 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526059,"numValue":-0.6347626006118983,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526060,"numValue":-1.5284917958017332,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526061,"numValue":0.4462638333867386,"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:19304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,304 | train | mutant | 727,760 | 358 | 727,951 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63A | V28H|V63A | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,556 | MegaScale | null | null | null | null | 0.380787 | null | null | null | null | null | null | -0.586307 | -1.55267 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526062,"numValue":-0.5863065682228679,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526063,"numValue":-1.5526697609888849,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526064,"numValue":0.3807871567410814,"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:19305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,305 | train | mutant | 727,761 | 358 | 727,952 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28H|V63G | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,557 | MegaScale | null | null | null | null | 0.40548 | null | null | null | null | null | null | -0.499957 | -1.584287 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526065,"numValue":-0.4999572934143606,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526066,"numValue":-1.584287385704517,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526067,"numValue":0.4054800841325199,"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:19307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,307 | train | mutant | 727,763 | 358 | 727,954 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28H|V63C | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,559 | MegaScale | null | null | null | null | 0.576573 | null | null | null | null | null | null | -0.58462 | -1.536001 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526071,"numValue":-0.5846202281365227,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526072,"numValue":-1.5360008307744804,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526073,"numValue":0.5765726702473504,"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:19309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,309 | train | mutant | 727,765 | 358 | 727,956 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28H|V63I | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,562 | MegaScale | null | null | null | null | 0.923653 | null | null | null | null | null | null | -0.31802 | -1.322847 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526080,"numValue":-0.3180197415818736,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526081,"numValue":-1.3228470348061871,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526082,"numValue":0.923653282729812,"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:19310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,310 | train | mutant | 727,766 | 358 | 727,957 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63W | V28H|V63W | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,563 | MegaScale | null | null | null | null | 0.240883 | null | null | null | null | null | null | -0.686155 | -2.000146 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526083,"numValue":-0.686155457754118,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526084,"numValue":-2.0001458678082864,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526085,"numValue":0.2408826208229982,"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:19311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,311 | train | mutant | 727,767 | 358 | 727,958 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Y | V28H|V63Y | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,564 | MegaScale | null | null | null | null | 0.198578 | null | null | null | null | null | null | -0.596165 | -1.999745 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526086,"numValue":-0.5961646561759841,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526087,"numValue":-1.9997450926705849,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526088,"numValue":0.1985776946023352,"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:19312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,312 | train | mutant | 727,768 | 358 | 727,959 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63F | V28H|V63F | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,565 | MegaScale | null | null | null | null | 0.317905 | null | null | null | null | null | null | -0.64478 | -1.869992 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526089,"numValue":-0.6447795931776905,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526090,"numValue":-1.869992323280976,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526091,"numValue":0.3179047307234949,"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:19313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,313 | train | mutant | 727,769 | 358 | 727,960 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63P | V28H|V63P | 2 | 2 | 0 | 0 | 28 | V | H | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,566 | MegaScale | null | null | null | null | 0.672507 | null | null | null | null | null | null | -0.236281 | -1.314449 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526092,"numValue":-0.2362805816429619,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526093,"numValue":-1.3144487160869214,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526094,"numValue":0.6725074114519282,"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:19314 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,314 | train | mutant | 727,770 | 358 | 727,961 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Q | V28D|V63Q | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,567 | MegaScale | null | null | null | null | -0.044932 | null | null | null | null | null | null | -0.620144 | -1.536603 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526095,"numValue":-0.6201443091046668,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526096,"numValue":-1.5366031527935402,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526097,"numValue":-0.0449321464802865,"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:19315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,315 | train | mutant | 727,771 | 358 | 727,962 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63E | V28D|V63E | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,568 | MegaScale | null | null | null | null | 0.151493 | null | null | null | null | null | null | -0.562931 | -1.466494 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526098,"numValue":-0.5629308985548036,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526099,"numValue":-1.4664943916215147,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526100,"numValue":0.1514926249287368,"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:19317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,317 | train | mutant | 727,773 | 358 | 727,964 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63H | V28D|V63H | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,570 | MegaScale | null | null | null | null | 0.256399 | null | null | null | null | null | null | -0.597904 | -1.407075 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526104,"numValue":-0.5979039679686662,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526105,"numValue":-1.4070748709541272,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526106,"numValue":0.2563985327806223,"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:19318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,318 | train | mutant | 727,774 | 358 | 727,965 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63D | V28D|V63D | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,571 | MegaScale | null | null | null | null | 0.255674 | null | null | null | null | null | null | -0.574551 | -1.39168 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526107,"numValue":-0.5745510437646512,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526108,"numValue":-1.3916795846392762,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526109,"numValue":0.2556740716939905,"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:19319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,319 | train | mutant | 727,775 | 358 | 727,966 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63R | V28D|V63R | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,572 | MegaScale | null | null | null | null | 0.143184 | null | null | null | null | null | null | -0.887285 | -1.533656 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526110,"numValue":-0.8872849254022808,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526111,"numValue":-1.5336563420319016,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526112,"numValue":0.1431839707726154,"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:19320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,320 | train | mutant | 727,776 | 358 | 727,967 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63K | V28D|V63K | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,573 | MegaScale | null | null | null | null | 0.411726 | null | null | null | null | null | null | -0.613642 | -1.364779 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526113,"numValue":-0.6136420885556807,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526114,"numValue":-1.3647787538644192,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526115,"numValue":0.4117263362344366,"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:19321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,321 | train | mutant | 727,777 | 358 | 727,968 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63T | V28D|V63T | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,574 | MegaScale | null | null | null | null | 0.270834 | null | null | null | null | null | null | -0.59674 | -1.381231 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526116,"numValue":-0.5967401172970817,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526117,"numValue":-1.3812309863688297,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526118,"numValue":0.2708339341577783,"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:19322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,322 | train | mutant | 727,778 | 358 | 727,969 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63S | V28D|V63S | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,575 | MegaScale | null | null | null | null | 0.209565 | null | null | null | null | null | null | -0.689682 | -1.46205 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526119,"numValue":-0.6896820280520413,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526120,"numValue":-1.4620496429962686,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526121,"numValue":0.2095653474157581,"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:19323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,323 | train | mutant | 727,779 | 358 | 727,970 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63A | V28D|V63A | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,576 | MegaScale | null | null | null | null | 0.226563 | null | null | null | null | null | null | -0.660457 | -1.423432 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526122,"numValue":-0.6604568115049233,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526123,"numValue":-1.4234321723732035,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526124,"numValue":0.2265630129724036,"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:19324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,324 | train | mutant | 727,780 | 358 | 727,971 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28D|V63G | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,577 | MegaScale | null | null | null | null | 0.010555 | null | null | null | null | null | null | -0.688613 | -1.502563 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526125,"numValue":-0.6886127332099703,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526126,"numValue":-1.5025631766977958,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526127,"numValue":0.0105545579713942,"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:19325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,325 | train | mutant | 727,781 | 358 | 727,972 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63M | V28D|V63M | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,578 | MegaScale | null | null | null | null | 0.187793 | null | null | null | null | null | null | -0.876588 | -1.432451 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526128,"numValue":-0.8765876764481013,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526129,"numValue":-1.4324513359179474,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526130,"numValue":0.1877933072827346,"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:19326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,326 | train | mutant | 727,782 | 358 | 727,973 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28D|V63C | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,579 | MegaScale | null | null | null | null | 0.401804 | null | null | null | null | null | null | -0.474975 | -1.499934 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526131,"numValue":-0.4749747627388169,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526132,"numValue":-1.4999336697795187,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526133,"numValue":0.4018039708599195,"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:19327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,327 | train | mutant | 727,783 | 358 | 727,974 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63L | V28D|V63L | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,580 | MegaScale | null | null | null | null | 0.217097 | null | null | null | null | null | null | -0.688754 | -1.466385 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526134,"numValue":-0.6887540375414407,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526135,"numValue":-1.4663852516891054,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526136,"numValue":0.2170971914332435,"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:19328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,328 | train | mutant | 727,784 | 358 | 727,975 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28D|V63I | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,582 | MegaScale | null | null | null | null | 0.320999 | null | null | null | null | null | null | -0.505656 | -1.483087 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526140,"numValue":-0.5056564126256748,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526141,"numValue":-1.4830872684701475,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526142,"numValue":0.3209987162775498,"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:19330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,330 | train | mutant | 727,786 | 358 | 727,977 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Y | V28D|V63Y | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,584 | MegaScale | null | null | null | null | -0.377803 | null | null | null | null | null | null | -0.828249 | -2.020846 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526146,"numValue":-0.8282490579938384,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526147,"numValue":-2.020846274322349,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526148,"numValue":-0.3778032453992198,"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:19331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,331 | train | mutant | 727,787 | 358 | 727,978 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63F | V28D|V63F | 2 | 2 | 0 | 0 | 28 | V | D | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,585 | MegaScale | null | null | null | null | -0.000558 | null | null | null | null | null | null | -0.915977 | -1.825966 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526149,"numValue":-0.9159772713658104,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526150,"numValue":-1.8259659797941037,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526151,"numValue":-0.0005578305354921,"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:19333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,333 | train | mutant | 727,789 | 358 | 727,980 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28R|V63Q | V28R|V63Q | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,587 | MegaScale | null | null | null | null | 0.08154 | null | null | null | null | null | null | -0.8105 | -1.961188 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526155,"numValue":-0.8105000626215185,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526156,"numValue":-1.9611878276990464,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526157,"numValue":0.0815397110558243,"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:19334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,334 | train | mutant | 727,790 | 358 | 727,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63E | V28R|V63E | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,588 | MegaScale | null | null | null | null | 0.278155 | null | null | null | null | null | null | -0.587944 | -1.844203 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526158,"numValue":-0.5879436090378738,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526159,"numValue":-1.8442027193627104,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526160,"numValue":0.2781547263923586,"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:19335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,335 | train | mutant | 727,791 | 358 | 727,982 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63N | V28R|V63N | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,589 | MegaScale | null | null | null | null | 0.202792 | null | null | null | null | null | null | -0.751853 | -1.892302 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526161,"numValue":-0.7518533773606575,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526162,"numValue":-1.8923023960178635,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526163,"numValue":0.2027915590856403,"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:19336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,336 | train | mutant | 727,792 | 358 | 727,983 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63H | V28R|V63H | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,590 | MegaScale | null | null | null | null | 0.621516 | null | null | null | null | null | null | -0.405832 | -1.756228 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526164,"numValue":-0.4058324746816957,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526165,"numValue":-1.7562275759660442,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526166,"numValue":0.6215164770271798,"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:19337 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,337 | train | mutant | 727,793 | 358 | 727,984 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63D | V28R|V63D | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,591 | MegaScale | null | null | null | null | -0.105988 | null | null | null | null | null | null | -0.757429 | -2.02319 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526167,"numValue":-0.7574289643317104,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526168,"numValue":-2.0231904371792697,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526169,"numValue":-0.1059884336447457,"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:19338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,338 | train | mutant | 727,794 | 358 | 727,985 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63R | V28R|V63R | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,592 | MegaScale | null | null | null | null | 0.205756 | null | null | null | null | null | null | -0.865855 | -1.905293 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526170,"numValue":-0.8658547204849139,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526171,"numValue":-1.905292930506763,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526172,"numValue":0.2057561857335907,"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:19339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,339 | train | mutant | 727,795 | 358 | 727,986 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63K | V28R|V63K | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,593 | MegaScale | null | null | null | null | 0.294251 | null | null | null | null | null | null | -0.781736 | -1.869888 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526173,"numValue":-0.781736208928876,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526174,"numValue":-1.869888106982762,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526175,"numValue":0.2942510599049974,"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:19340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,340 | train | mutant | 727,796 | 358 | 727,987 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63T | V28R|V63T | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,594 | MegaScale | null | null | null | null | 0.278925 | null | null | null | null | null | null | -0.698306 | -1.846433 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526176,"numValue":-0.6983061083760939,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526177,"numValue":-1.846432574937738,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526178,"numValue":0.2789248305428752,"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:19341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,341 | train | mutant | 727,797 | 358 | 727,988 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63S | V28R|V63S | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,595 | MegaScale | null | null | null | null | 0.17708 | null | null | null | null | null | null | -0.699354 | -1.922039 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526179,"numValue":-0.6993539995442069,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526180,"numValue":-1.9220391482274928,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526181,"numValue":0.1770797039620551,"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:19342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,342 | train | mutant | 727,798 | 358 | 727,989 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63A | V28R|V63A | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,596 | MegaScale | null | null | null | null | 0.257135 | null | null | null | null | null | null | -0.779828 | -1.843537 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526182,"numValue":-0.7798278015130662,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526183,"numValue":-1.84353708463196,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526184,"numValue":0.2571352710927237,"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:19343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,343 | train | mutant | 727,799 | 358 | 727,990 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28R|V63G | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,597 | MegaScale | null | null | null | null | 0.301975 | null | null | null | null | null | null | -0.684901 | -1.908136 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526185,"numValue":-0.6849005047098393,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526186,"numValue":-1.9081355453219733,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526187,"numValue":0.3019754603841573,"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:19344 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,344 | train | mutant | 727,800 | 358 | 727,991 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63M | V28R|V63M | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,598 | MegaScale | null | null | null | null | 0.194254 | null | null | null | null | null | null | -0.88197 | -1.935651 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526188,"numValue":-0.8819696983518874,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526189,"numValue":-1.9356506065483248,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526190,"numValue":0.1942535623983242,"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:19345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,345 | train | mutant | 727,801 | 358 | 727,992 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28R|V63C | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,599 | MegaScale | null | null | null | null | 0.412472 | null | null | null | null | null | null | -0.516789 | -1.895706 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526191,"numValue":-0.5167893422275287,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526192,"numValue":-1.8957063758585255,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526193,"numValue":0.4124722963984423,"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:19346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,346 | train | mutant | 727,802 | 358 | 727,993 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63L | V28R|V63L | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,600 | MegaScale | null | null | null | null | 0.281624 | null | null | null | null | null | null | -0.732207 | -1.962218 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526194,"numValue":-0.7322069807625535,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526195,"numValue":-1.9622177261624127,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526196,"numValue":0.2816237719436834,"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:19347 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,347 | train | mutant | 727,803 | 358 | 727,994 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28R|V63I | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,602 | MegaScale | null | null | null | null | 0.309731 | null | null | null | null | null | null | -0.712374 | -1.828171 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526200,"numValue":-0.7123736257748607,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526201,"numValue":-1.8281705848520453,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526202,"numValue":0.3097311317843161,"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:19348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,348 | train | mutant | 727,804 | 358 | 727,995 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63W | V28R|V63W | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,603 | MegaScale | null | null | null | null | 0.135023 | null | null | null | null | null | null | -0.754494 | -2.115892 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526203,"numValue":-0.7544944901319476,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526204,"numValue":-2.11589248226635,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526205,"numValue":0.1350226616061916,"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:19349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,349 | train | mutant | 727,805 | 358 | 727,996 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Y | V28R|V63Y | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,604 | MegaScale | null | null | null | null | -0.058747 | null | null | null | null | null | null | -0.745768 | -2.230059 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526206,"numValue":-0.745768047548492,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526207,"numValue":-2.230059381309545,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526208,"numValue":-0.0587471803888324,"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:19350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,350 | train | mutant | 727,806 | 358 | 727,997 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63F | V28R|V63F | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,605 | MegaScale | null | null | null | null | 0.237467 | null | null | null | null | null | null | -0.608467 | -2.111512 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526209,"numValue":-0.6084673164051191,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526210,"numValue":-2.1115122531957224,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526211,"numValue":0.2374672135222733,"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:19351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,351 | train | mutant | 727,807 | 358 | 727,998 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63P | V28R|V63P | 2 | 2 | 0 | 0 | 28 | V | R | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,606 | MegaScale | null | null | null | null | 0.221548 | null | null | null | null | null | null | -0.756627 | -1.869971 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526212,"numValue":-0.7566269002727135,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526213,"numValue":-1.8699706980355757,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526214,"numValue":0.2215484894155648,"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:19352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,352 | train | mutant | 727,808 | 358 | 727,999 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Q | V28K|V63Q | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,607 | MegaScale | null | null | null | null | 0.445393 | null | null | null | null | null | null | -0.58441 | -1.709211 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526215,"numValue":-0.5844095719052067,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526216,"numValue":-1.709210598131561,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526217,"numValue":0.4453933060014886,"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:19353 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,353 | train | mutant | 727,809 | 358 | 728,000 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63E | V28K|V63E | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,608 | MegaScale | null | null | null | null | 0.38514 | null | null | null | null | null | null | -0.55495 | -1.662352 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526218,"numValue":-0.5549504873967614,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526219,"numValue":-1.6623521387448497,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526220,"numValue":0.3851401662679415,"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:19355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,355 | train | mutant | 727,811 | 358 | 728,002 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63H | V28K|V63H | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,610 | MegaScale | null | null | null | null | 0.101727 | null | null | null | null | null | null | -0.649397 | -1.888688 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526224,"numValue":-0.649396616957084,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526225,"numValue":-1.8886881988662456,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526226,"numValue":0.1017265459589979,"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:19357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,357 | train | mutant | 727,813 | 358 | 728,004 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63R | V28K|V63R | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,612 | MegaScale | null | null | null | null | 0.328082 | null | null | null | null | null | null | -0.839307 | -1.759237 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526230,"numValue":-0.8393072485902289,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526231,"numValue":-1.759236889620713,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526232,"numValue":0.3280820528938549,"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:19358 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,358 | train | mutant | 727,814 | 358 | 728,005 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63K | V28K|V63K | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,613 | MegaScale | null | null | null | null | 0.324567 | null | null | null | null | null | null | -0.701176 | -1.75094 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526233,"numValue":-0.7011761763127875,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526234,"numValue":-1.7509396658079153,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526235,"numValue":0.3245671862247944,"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:19359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,359 | train | mutant | 727,815 | 358 | 728,006 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63T | V28K|V63T | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,614 | MegaScale | null | null | null | null | 0.434004 | null | null | null | null | null | null | -0.528536 | -1.615747 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526236,"numValue":-0.5285357233672723,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526237,"numValue":-1.615747191066658,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526238,"numValue":0.4340038144101718,"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:19360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,360 | train | mutant | 727,816 | 358 | 728,007 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63S | V28K|V63S | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,615 | MegaScale | null | null | null | null | 0.549049 | null | null | null | null | null | null | -0.651345 | -1.602549 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526239,"numValue":-0.6513450042014295,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526240,"numValue":-1.6025491190133168,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526241,"numValue":0.5490488645239873,"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:19361 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,361 | train | mutant | 727,817 | 358 | 728,008 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63A | V28K|V63A | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,616 | MegaScale | null | null | null | null | 0.290309 | null | null | null | null | null | null | -0.601005 | -1.797676 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526242,"numValue":-0.6010054708968592,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526243,"numValue":-1.797675711349771,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526244,"numValue":0.2903092831156112,"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:19362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,362 | train | mutant | 727,818 | 358 | 728,009 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28K|V63G | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,617 | MegaScale | null | null | null | null | 0.425375 | null | null | null | null | null | null | -0.556387 | -1.73402 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526245,"numValue":-0.5563874956624315,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526246,"numValue":-1.7340204325174584,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526247,"numValue":0.4253750618510926,"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:19363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,363 | train | mutant | 727,819 | 358 | 728,010 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63M | V28K|V63M | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,618 | MegaScale | null | null | null | null | 0.010221 | null | null | null | null | null | null | -0.894467 | -1.845013 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526248,"numValue":-0.8944673384570251,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526249,"numValue":-1.8450129690965231,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526250,"numValue":0.0102214294820232,"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:19364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,364 | train | mutant | 727,820 | 358 | 728,011 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28K|V63C | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,619 | MegaScale | null | null | null | null | 0.454043 | null | null | null | null | null | null | -0.493368 | -1.708013 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526251,"numValue":-0.493368278207048,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526252,"numValue":-1.7080130922510752,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526253,"numValue":0.4540429313356668,"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:19365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,365 | train | mutant | 727,821 | 358 | 728,012 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63L | V28K|V63L | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,620 | MegaScale | null | null | null | null | 0.304477 | null | null | null | null | null | null | -0.636506 | -1.813649 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526254,"numValue":-0.6365056023745727,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526255,"numValue":-1.8136493632998771,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526256,"numValue":0.3044765933645974,"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:19366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,366 | train | mutant | 727,822 | 358 | 728,013 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28K|V63I | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,622 | MegaScale | null | null | null | null | 0.395947 | null | null | null | null | null | null | -0.566726 | -1.668247 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526260,"numValue":-0.5667260905751277,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526261,"numValue":-1.6682466527469448,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526262,"numValue":0.3959472134449565,"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:19367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,367 | train | mutant | 727,823 | 358 | 728,014 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63W | V28K|V63W | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,623 | MegaScale | null | null | null | null | 0.027811 | null | null | null | null | null | null | -0.685311 | -2.122745 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526263,"numValue":-0.6853106218031448,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526264,"numValue":-2.1227447700526145,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526265,"numValue":0.0278109603880084,"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:19368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,368 | train | mutant | 727,824 | 358 | 728,015 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Y | V28K|V63Y | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,624 | MegaScale | null | null | null | null | 0.075823 | null | null | null | null | null | null | -0.756996 | -2.11741 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526266,"numValue":-0.756996215588776,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526267,"numValue":-2.117409707695164,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526268,"numValue":0.0758226812416479,"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:19369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,369 | train | mutant | 727,825 | 358 | 728,016 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63F | V28K|V63F | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,625 | MegaScale | null | null | null | null | -0.03768 | null | null | null | null | null | null | -0.818371 | -2.078477 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526269,"numValue":-0.8183710389531937,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526270,"numValue":-2.078477336998891,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526271,"numValue":-0.0376803255660986,"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:19370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,370 | train | mutant | 727,826 | 358 | 728,017 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63P | V28K|V63P | 2 | 2 | 0 | 0 | 28 | V | K | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,626 | MegaScale | null | null | null | null | 0.392754 | null | null | null | null | null | null | -0.561167 | -1.637694 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526272,"numValue":-0.5611673995740767,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526273,"numValue":-1.6376941009376336,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526274,"numValue":0.3927536607990115,"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:19371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,371 | train | mutant | 727,827 | 358 | 728,018 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Q | V28T|V63Q | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,627 | MegaScale | null | null | null | null | 0.206633 | null | null | null | null | null | null | -0.569891 | -1.80533 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526275,"numValue":-0.5698908135818601,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526276,"numValue":-1.8053299088563783,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526277,"numValue":0.2066326598661588,"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:19372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,372 | train | mutant | 727,828 | 358 | 728,019 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63E | V28T|V63E | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,628 | MegaScale | null | null | null | null | 0.126387 | null | null | null | null | null | null | -0.578014 | -1.804989 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526278,"numValue":-0.5780135328755569,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526279,"numValue":-1.8049893846409697,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526280,"numValue":0.1263871931081825,"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:19373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,373 | train | mutant | 727,829 | 358 | 728,020 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63N | V28T|V63N | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,629 | MegaScale | null | null | null | null | 0.231687 | null | null | null | null | null | null | -0.682339 | -1.718897 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526281,"numValue":-0.6823393724443636,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526282,"numValue":-1.718897174409543,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526283,"numValue":0.2316870025523402,"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:19374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,374 | train | mutant | 727,830 | 358 | 728,021 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63H | V28T|V63H | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,630 | MegaScale | null | null | null | null | 0.415553 | null | null | null | null | null | null | -0.496857 | -1.677546 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526284,"numValue":-0.4968571707065694,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526285,"numValue":-1.6775464211687927,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526286,"numValue":0.4155528848888121,"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:19375 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,375 | train | mutant | 727,831 | 358 | 728,022 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63D | V28T|V63D | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,631 | MegaScale | null | null | null | null | 0.371996 | null | null | null | null | null | null | -0.612888 | -1.664575 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526287,"numValue":-0.6128877332129472,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526288,"numValue":-1.6645745669198533,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526289,"numValue":0.3719964489874505,"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:19376 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,376 | train | mutant | 727,832 | 358 | 728,023 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63R | V28T|V63R | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,632 | MegaScale | null | null | null | null | 0.428857 | null | null | null | null | null | null | -0.746126 | -1.749401 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526290,"numValue":-0.7461256261984289,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526291,"numValue":-1.749401170346406,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526292,"numValue":0.4288567508263231,"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:19377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,377 | train | mutant | 727,833 | 358 | 728,024 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63K | V28T|V63K | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,633 | MegaScale | null | null | null | null | 0.085284 | null | null | null | null | null | null | -0.747504 | -1.848186 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526293,"numValue":-0.7475042053015574,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526294,"numValue":-1.848186174978777,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526295,"numValue":0.0852835887339844,"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:19379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,379 | train | mutant | 727,835 | 358 | 728,026 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63S | V28T|V63S | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,635 | MegaScale | null | null | null | null | 0.459409 | null | null | null | null | null | null | -0.40349 | -1.734973 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526299,"numValue":-0.4034899722509359,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526300,"numValue":-1.7349728047299542,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526301,"numValue":0.4594092039467639,"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:19380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,380 | train | mutant | 727,836 | 358 | 728,027 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63A | V28T|V63A | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,636 | MegaScale | null | null | null | null | 0.901069 | null | null | null | null | null | null | -0.165554 | -1.438873 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526302,"numValue":-0.1655542233204993,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526303,"numValue":-1.438872661940524,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526304,"numValue":0.9010685423693472,"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:19381 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,381 | train | mutant | 727,837 | 358 | 728,028 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28T|V63G | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,637 | MegaScale | null | null | null | null | 0.639655 | null | null | null | null | null | null | -0.535164 | -1.556833 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526305,"numValue":-0.5351640997196738,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526306,"numValue":-1.5568330631045062,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526307,"numValue":0.6396547287030554,"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:19382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,382 | train | mutant | 727,838 | 358 | 728,029 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63M | V28T|V63M | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,638 | MegaScale | null | null | null | null | 2.10496 | null | null | null | null | null | null | 0.477951 | -0.660698 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526308,"numValue":0.4779511588102045,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526309,"numValue":-0.6606980212547284,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526310,"numValue":2.1049599342100827,"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:19383 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,383 | train | mutant | 727,839 | 358 | 728,030 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28T|V63C | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,639 | MegaScale | null | null | null | null | 0.818674 | null | null | null | null | null | null | -0.288627 | -1.581162 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526311,"numValue":-0.2886268789853845,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526312,"numValue":-1.5811619836578048,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526313,"numValue":0.8186737469903793,"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:19384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,384 | train | mutant | 727,840 | 358 | 728,031 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63L | V28T|V63L | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,640 | MegaScale | null | null | null | null | 3.430958 | null | null | null | null | null | null | 1.225425 | 0.313509 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526314,"numValue":1.2254250739971166,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526315,"numValue":0.3135087290726431,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526316,"numValue":3.4309576043038432,"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:19385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,385 | train | mutant | 727,841 | 358 | 728,032 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28T|V63I | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,642 | MegaScale | null | null | null | null | 3.200721 | null | null | null | null | null | null | 1.207114 | 0.179121 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526320,"numValue":1.2071140249170091,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526321,"numValue":0.1791208785304359,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526322,"numValue":3.200720529957924,"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:19387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,387 | train | mutant | 727,843 | 358 | 728,034 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Y | V28T|V63Y | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,644 | MegaScale | null | null | null | null | 0.057831 | null | null | null | null | null | null | -0.761124 | -2.032118 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526326,"numValue":-0.761123755701929,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526327,"numValue":-2.0321178554243007,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526328,"numValue":0.0578309291851112,"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:19388 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,388 | train | mutant | 727,844 | 358 | 728,035 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63F | V28T|V63F | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,645 | MegaScale | null | null | null | null | 0.310474 | null | null | null | null | null | null | -0.776663 | -1.922352 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526329,"numValue":-0.776662824823144,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526330,"numValue":-1.922351819337874,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526331,"numValue":0.31047354643043,"references":[],"strValue":null,"typ... | [{"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:19389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,389 | train | mutant | 727,845 | 358 | 728,036 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63P | V28T|V63P | 2 | 2 | 0 | 0 | 28 | V | T | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,646 | MegaScale | null | null | null | null | 0.294504 | null | null | null | null | null | null | -0.44976 | -1.717509 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526332,"numValue":-0.4497598448337828,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526333,"numValue":-1.7175088123249749,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526334,"numValue":0.2945036647559307,"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:19390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,390 | train | mutant | 727,846 | 358 | 728,037 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Q | V28S|V63Q | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,647 | MegaScale | null | null | null | null | 0.119656 | null | null | null | null | null | null | -0.596788 | -1.819578 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526335,"numValue":-0.5967882356294106,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526336,"numValue":-1.8195784831994404,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526337,"numValue":0.1196558865767426,"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:19392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,392 | train | mutant | 727,848 | 358 | 728,039 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63N | V28S|V63N | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,649 | MegaScale | null | null | null | null | 0.09871 | null | null | null | null | null | null | -0.705788 | -1.800909 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526341,"numValue":-0.7057876704226198,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526342,"numValue":-1.8009091237404902,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526343,"numValue":0.0987095257482684,"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:19393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,393 | train | mutant | 727,849 | 358 | 728,040 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63H | V28S|V63H | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,650 | MegaScale | null | null | null | null | 0.257976 | null | null | null | null | null | null | -0.638133 | -1.773876 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526344,"numValue":-0.6381328353776231,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526345,"numValue":-1.7738758025258288,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526346,"numValue":0.2579755713159491,"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:19394 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,394 | train | mutant | 727,850 | 358 | 728,041 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63D | V28S|V63D | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,651 | MegaScale | null | null | null | null | 0.034881 | null | null | null | null | null | null | -0.679053 | -1.814562 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526347,"numValue":-0.6790530574001816,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526348,"numValue":-1.8145619611793,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526349,"numValue":0.0348805220510944,"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:19395 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,395 | train | mutant | 727,851 | 358 | 728,042 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63R | V28S|V63R | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,652 | MegaScale | null | null | null | null | -0.04586 | null | null | null | null | null | null | -0.99705 | -1.922272 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526350,"numValue":-0.9970502653079768,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526351,"numValue":-1.9222719375594368,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526352,"numValue":-0.0458600483838517,"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:19396 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,396 | train | mutant | 727,852 | 358 | 728,043 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63K | V28S|V63K | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,653 | MegaScale | null | null | null | null | 0.227404 | null | null | null | null | null | null | -0.729932 | -1.753083 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526353,"numValue":-0.7299318742969967,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526354,"numValue":-1.7530826535001254,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526355,"numValue":0.227403757475371,"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:19399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,399 | train | mutant | 727,855 | 358 | 728,046 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63A | V28S|V63A | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,656 | MegaScale | null | null | null | null | 0.129473 | null | null | null | null | null | null | -0.68984 | -1.806041 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526362,"numValue":-0.689840182472675,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526363,"numValue":-1.806040922325024,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526364,"numValue":0.1294731812721998,"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:19400 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,400 | train | mutant | 727,856 | 358 | 728,047 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28S|V63G | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,657 | MegaScale | null | null | null | null | 0.170587 | null | null | null | null | null | null | -0.659736 | -1.810649 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526365,"numValue":-0.6597356443125018,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526366,"numValue":-1.810649353244144,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526367,"numValue":0.1705868514234945,"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:19401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,401 | train | mutant | 727,857 | 358 | 728,048 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63M | V28S|V63M | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,658 | MegaScale | null | null | null | null | 0.687552 | null | null | null | null | null | null | -0.482391 | -1.548278 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526368,"numValue":-0.4823912579262667,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526369,"numValue":-1.5482777681909077,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526370,"numValue":0.6875523298776662,"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:19402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,402 | train | mutant | 727,858 | 358 | 728,049 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28S|V63C | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,659 | MegaScale | null | null | null | null | 0.308919 | null | null | null | null | null | null | -0.488146 | -1.792159 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526371,"numValue":-0.4881464173493532,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526372,"numValue":-1.792158654242448,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526373,"numValue":0.3089187612688805,"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:19403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,403 | train | mutant | 727,859 | 358 | 728,050 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63L | V28S|V63L | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,660 | MegaScale | null | null | null | null | 1.585246 | null | null | null | null | null | null | 0.061047 | -1.01558 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526374,"numValue":0.0610466340566789,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526375,"numValue":-1.0155804956835297,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526376,"numValue":1.5852463551629028,"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:19404 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,404 | train | mutant | 727,860 | 358 | 728,051 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28S|V63I | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,662 | MegaScale | null | null | null | null | 2.714115 | null | null | null | null | null | null | 0.942128 | -0.171273 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526380,"numValue":0.9421281663519204,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526381,"numValue":-0.1712730992389638,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526382,"numValue":2.7141154521383903,"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:19405 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,405 | train | mutant | 727,861 | 358 | 728,052 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63W | V28S|V63W | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,663 | MegaScale | null | null | null | null | -0.112976 | null | null | null | null | null | null | -0.85872 | -2.225277 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526383,"numValue":-0.8587199385353517,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526384,"numValue":-2.225277269843563,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526385,"numValue":-0.1129763464895016,"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:19407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,407 | train | mutant | 727,863 | 358 | 728,054 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63F | V28S|V63F | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,665 | MegaScale | null | null | null | null | -0.03542 | null | null | null | null | null | null | -0.817115 | -2.044351 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526389,"numValue":-0.8171148792081299,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526390,"numValue":-2.0443507639142,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526391,"numValue":-0.0354199236289074,"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:19408 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,408 | train | mutant | 727,864 | 358 | 728,055 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63P | V28S|V63P | 2 | 2 | 0 | 0 | 28 | V | S | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,666 | MegaScale | null | null | null | null | -0.064068 | null | null | null | null | null | null | -0.563867 | -1.862551 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526392,"numValue":-0.563867048231435,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526393,"numValue":-1.8625513368039603,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526394,"numValue":-0.0640682877385013,"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:19409 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,409 | train | mutant | 727,865 | 358 | 728,056 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Q | V28A|V63Q | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,667 | MegaScale | null | null | null | null | 0.281639 | null | null | null | null | null | null | -0.605023 | -1.766283 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526395,"numValue":-0.6050228566628877,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526396,"numValue":-1.7662828410103062,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526397,"numValue":0.2816390277615936,"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:19410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,410 | train | mutant | 727,866 | 358 | 728,057 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63E | V28A|V63E | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,668 | MegaScale | null | null | null | null | 0.615451 | null | null | null | null | null | null | -0.452756 | -1.486964 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526398,"numValue":-0.4527555003851259,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526399,"numValue":-1.486963937341601,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526400,"numValue":0.6154513910043486,"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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