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:19521 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,521 | train | mutant | 727,977 | 358 | 728,168 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28I|V63F | V28I|V63F | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,804 | MegaScale | null | null | null | null | 1.29444 | null | null | null | null | null | null | -0.037173 | -1.351816 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526806,"numValue":-0.0371733047050959,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526807,"numValue":-1.351815522358952,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526808,"numValue":1.2944400802914582,"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:19522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,522 | train | mutant | 727,978 | 358 | 728,169 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28I|V63P | V28I|V63P | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,805 | MegaScale | null | null | null | null | 1.56006 | null | null | null | null | null | null | 0.117575 | -0.901149 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526809,"numValue":0.1175753594395546,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526810,"numValue":-0.9011485647035514,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526811,"numValue":1.5600604016064443,"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:19523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,523 | train | mutant | 727,979 | 358 | 728,170 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63Q | V28W|V63Q | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,806 | MegaScale | null | null | null | null | 0.88007 | null | null | null | null | null | null | -0.50568 | -1.427438 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526812,"numValue":-0.505680176947859,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526813,"numValue":-1.4274375590858828,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526814,"numValue":0.8800700128249705,"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:19524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,524 | train | mutant | 727,980 | 358 | 728,171 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63E | V28W|V63E | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,807 | MegaScale | null | null | null | null | 0.953915 | null | null | null | null | null | null | -0.373057 | -1.354138 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526815,"numValue":-0.3730568843924995,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526816,"numValue":-1.354137910808317,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526817,"numValue":0.9539149649195358,"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:19525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,525 | train | mutant | 727,981 | 358 | 728,172 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63N | V28W|V63N | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,808 | MegaScale | null | null | null | null | 0.960504 | null | null | null | null | null | null | -0.408998 | -1.392284 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526818,"numValue":-0.4089983164670454,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526819,"numValue":-1.3922843244520142,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526820,"numValue":0.9605041734578031,"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:19526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,526 | train | mutant | 727,982 | 358 | 728,173 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63H | V28W|V63H | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,809 | MegaScale | null | null | null | null | 0.805904 | null | null | null | null | null | null | -0.484343 | -1.477418 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526821,"numValue":-0.4843425306088919,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526822,"numValue":-1.477418185620328,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526823,"numValue":0.8059037517548051,"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:19527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,527 | train | mutant | 727,983 | 358 | 728,174 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63D | V28W|V63D | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,810 | MegaScale | null | null | null | null | 0.997969 | null | null | null | null | null | null | -0.316281 | -1.399545 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526824,"numValue":-0.3162810385446957,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526825,"numValue":-1.3995450444703796,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526826,"numValue":0.9979691836321396,"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:19528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,528 | train | mutant | 727,984 | 358 | 728,175 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63R | V28W|V63R | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,811 | MegaScale | null | null | null | null | 0.937337 | null | null | null | null | null | null | -0.664302 | -1.429373 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526827,"numValue":-0.6643024771593679,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526828,"numValue":-1.429373200572468,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526829,"numValue":0.9373365114622128,"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:19529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,529 | train | mutant | 727,985 | 358 | 728,176 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63K | V28W|V63K | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,812 | MegaScale | null | null | null | null | 0.971871 | null | null | null | null | null | null | -0.482495 | -1.409272 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526830,"numValue":-0.482495167319375,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526831,"numValue":-1.4092715273361869,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526832,"numValue":0.9718712526235496,"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:19530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,530 | train | mutant | 727,986 | 358 | 728,177 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63T | V28W|V63T | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,813 | MegaScale | null | null | null | null | 1.049858 | null | null | null | null | null | null | -0.216641 | -1.339472 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526833,"numValue":-0.2166405904330039,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526834,"numValue":-1.339472117692047,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526835,"numValue":1.04985796080705,"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:19531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,531 | train | mutant | 727,987 | 358 | 728,178 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63S | V28W|V63S | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,814 | MegaScale | null | null | null | null | 1.015349 | null | null | null | null | null | null | -0.378757 | -1.396565 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526836,"numValue":-0.3787568568380404,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526837,"numValue":-1.3965651248221755,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526838,"numValue":1.0153490779343357,"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:19532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,532 | train | mutant | 727,988 | 358 | 728,179 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63A | V28W|V63A | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,815 | MegaScale | null | null | null | null | 1.095864 | null | null | null | null | null | null | -0.370089 | -1.359346 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526839,"numValue":-0.3700887838045376,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526840,"numValue":-1.359345907580651,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526841,"numValue":1.095864106586732,"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:19535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,535 | train | mutant | 727,991 | 358 | 728,182 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63C | V28W|V63C | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,818 | MegaScale | null | null | null | null | 1.431392 | null | null | null | null | null | null | 0.057736 | -1.147189 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526848,"numValue":0.0577362369705686,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526849,"numValue":-1.147188780165925,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526850,"numValue":1.4313920393575763,"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:19536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,536 | train | mutant | 727,992 | 358 | 728,183 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63L | V28W|V63L | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,819 | MegaScale | null | null | null | null | 2.380997 | null | null | null | null | null | null | 0.48827 | -0.478175 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526851,"numValue":0.4882698299525282,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526852,"numValue":-0.4781748224743464,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526853,"numValue":2.3809972820253664,"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:19537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,537 | train | mutant | 727,993 | 358 | 728,184 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63I | V28W|V63I | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,821 | MegaScale | null | null | null | null | 3.433298 | null | null | null | null | null | null | 1.247203 | 0.271097 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526857,"numValue":1.247202903691429,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526858,"numValue":0.2710967947405361,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526859,"numValue":3.433297643598438,"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:19538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,538 | train | mutant | 727,994 | 358 | 728,185 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63W | V28W|V63W | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,822 | MegaScale | null | null | null | null | 0.582479 | null | null | null | null | null | null | -0.587237 | -1.879018 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526860,"numValue":-0.5872369915158369,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526861,"numValue":-1.8790178556307708,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526862,"numValue":0.5824786173171446,"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:19540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,540 | train | mutant | 727,996 | 358 | 728,187 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63F | V28W|V63F | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,824 | MegaScale | null | null | null | null | 0.916203 | null | null | null | null | null | null | -0.39116 | -1.582701 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526866,"numValue":-0.3911599902277414,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526867,"numValue":-1.5827010282980538,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526868,"numValue":0.9162025695564118,"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:19541 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,541 | train | mutant | 727,997 | 358 | 728,188 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28W|V63P | V28W|V63P | 2 | 2 | 0 | 0 | 28 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,825 | MegaScale | null | null | null | null | 0.978268 | null | null | null | null | null | null | -0.342025 | -1.406392 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526869,"numValue":-0.3420254603337971,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526870,"numValue":-1.4063920437596291,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526871,"numValue":0.978268132938946,"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:19542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,542 | train | mutant | 727,998 | 358 | 728,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63Q | V28Y|V63Q | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,826 | MegaScale | null | null | null | null | 1.033155 | null | null | null | null | null | null | -0.45935 | -1.228005 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526872,"numValue":-0.4593499169094958,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526873,"numValue":-1.2280046264828122,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526874,"numValue":1.033154892959652,"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:19543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,543 | train | mutant | 727,999 | 358 | 728,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63E | V28Y|V63E | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,827 | MegaScale | null | null | null | null | 1.032136 | null | null | null | null | null | null | -0.315352 | -1.231346 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526875,"numValue":-0.3153522644307424,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526876,"numValue":-1.2313460246579615,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526877,"numValue":1.0321357461297969,"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:19544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,544 | train | mutant | 728,000 | 358 | 728,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63N | V28Y|V63N | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,828 | MegaScale | null | null | null | null | 0.952067 | null | null | null | null | null | null | -0.406705 | -1.266057 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526878,"numValue":-0.4067050701407823,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526879,"numValue":-1.2660573717603731,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526880,"numValue":0.952067387231946,"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:19545 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,545 | train | mutant | 728,001 | 358 | 728,192 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63H | V28Y|V63H | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,829 | MegaScale | null | null | null | null | 1.043568 | null | null | null | null | null | null | -0.443341 | -1.192114 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526881,"numValue":-0.4433407492591169,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526882,"numValue":-1.1921136843738993,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526883,"numValue":1.043568402699634,"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:19546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,546 | train | mutant | 728,002 | 358 | 728,193 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63D | V28Y|V63D | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,830 | MegaScale | null | null | null | null | 0.904966 | null | null | null | null | null | null | -0.411111 | -1.296643 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526884,"numValue":-0.4111110006320924,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526885,"numValue":-1.2966426320626687,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526886,"numValue":0.904966403273502,"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:19548 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,548 | train | mutant | 728,004 | 358 | 728,195 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63K | V28Y|V63K | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,832 | MegaScale | null | null | null | null | 0.93134 | null | null | null | null | null | null | -0.503853 | -1.285934 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526890,"numValue":-0.5038530031119683,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526891,"numValue":-1.285934343259588,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526892,"numValue":0.9313399366293044,"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:19549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,549 | train | mutant | 728,005 | 358 | 728,196 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63T | V28Y|V63T | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,833 | MegaScale | null | null | null | null | 1.07272 | null | null | null | null | null | null | -0.337221 | -1.173981 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526893,"numValue":-0.3372208326524569,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526894,"numValue":-1.1739812296917562,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526895,"numValue":1.0727204931356016,"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:19550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,550 | train | mutant | 728,006 | 358 | 728,197 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63S | V28Y|V63S | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,834 | MegaScale | null | null | null | null | 0.992611 | null | null | null | null | null | null | -0.38135 | -1.244415 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526896,"numValue":-0.3813503766487876,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526897,"numValue":-1.2444147191080672,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526898,"numValue":0.9926113887527962,"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:19551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,551 | train | mutant | 728,007 | 358 | 728,198 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63A | V28Y|V63A | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,835 | MegaScale | null | null | null | null | 1.231233 | null | null | null | null | null | null | -0.652773 | -1.095599 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526899,"numValue":-0.6527729817240673,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526900,"numValue":-1.0955994877457371,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526901,"numValue":1.2312325938903164,"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:19553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,553 | train | mutant | 728,009 | 358 | 728,200 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63M | V28Y|V63M | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,837 | MegaScale | null | null | null | null | 2.541185 | null | null | null | null | null | null | 0.422481 | -0.28454 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526905,"numValue":0.4224809829243653,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526906,"numValue":-0.2845401743605633,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526907,"numValue":2.541184906995789,"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:19554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,554 | train | mutant | 728,010 | 358 | 728,201 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63C | V28Y|V63C | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,838 | MegaScale | null | null | null | null | 1.673956 | null | null | null | null | null | null | -0.084203 | -0.774315 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526908,"numValue":-0.0842026993456731,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526909,"numValue":-0.7743147219600381,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526910,"numValue":1.673955618223343,"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:19555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,555 | train | mutant | 728,011 | 358 | 728,202 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63L | V28Y|V63L | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,839 | MegaScale | null | null | null | null | 2.898464 | null | null | null | null | null | null | 0.734282 | -0.023809 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526911,"numValue":0.7342819561040898,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526912,"numValue":-0.0238091610615045,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526913,"numValue":2.898464164763594,"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:19556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,556 | train | mutant | 728,012 | 358 | 728,203 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63I | V28Y|V63I | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,841 | MegaScale | null | null | null | null | 3.853325 | null | null | null | null | null | null | 1.543838 | 0.625307 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526917,"numValue":1.5438380649667574,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526918,"numValue":0.6253070778694578,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526919,"numValue":3.853324780859914,"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:19557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,557 | train | mutant | 728,013 | 358 | 728,204 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63W | V28Y|V63W | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,842 | MegaScale | null | null | null | null | 0.51064 | null | null | null | null | null | null | -0.615393 | -1.836352 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526920,"numValue":-0.6153925553827588,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526921,"numValue":-1.8363523264415795,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526922,"numValue":0.5106401459216938,"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:19558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,558 | train | mutant | 728,014 | 358 | 728,205 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63Y | V28Y|V63Y | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,843 | MegaScale | null | null | null | null | 0.640166 | null | null | null | null | null | null | -0.378121 | -1.841811 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526923,"numValue":-0.3781205591077662,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526924,"numValue":-1.8418114055163537,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526925,"numValue":0.6401655630553191,"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:19559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,559 | train | mutant | 728,015 | 358 | 728,206 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63F | V28Y|V63F | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,844 | MegaScale | null | null | null | null | 0.766603 | null | null | null | null | null | null | -0.391014 | -1.701789 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526926,"numValue":-0.3910137264036163,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526927,"numValue":-1.7017892449136416,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526928,"numValue":0.7666032044366917,"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:19560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,560 | train | mutant | 728,016 | 358 | 728,207 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28Y|V63P | V28Y|V63P | 2 | 2 | 0 | 0 | 28 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,845 | MegaScale | null | null | null | null | 1.096907 | null | null | null | null | null | null | -0.275515 | -1.130612 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526929,"numValue":-0.2755148164596187,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526930,"numValue":-1.1306120079702402,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526931,"numValue":1.096907376758625,"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:19561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,561 | train | mutant | 728,017 | 358 | 728,208 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63Q | V28F|V63Q | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,846 | MegaScale | null | null | null | null | 1.836797 | null | null | null | null | null | null | -0.037831 | -0.645092 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526932,"numValue":-0.0378313102668907,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526933,"numValue":-0.6450916721551665,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526934,"numValue":1.8367974133554383,"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:19562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,562 | train | mutant | 728,018 | 358 | 728,209 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63E | V28F|V63E | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,847 | MegaScale | null | null | null | null | 1.700847 | null | null | null | null | null | null | 0.000525 | -0.768955 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526935,"numValue":0.0005249717783521,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526936,"numValue":-0.7689546543892762,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526937,"numValue":1.7008473356748706,"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:19563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,563 | train | mutant | 728,019 | 358 | 728,210 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63N | V28F|V63N | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,848 | MegaScale | null | null | null | null | 1.732129 | null | null | null | null | null | null | -0.029643 | -0.766068 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526938,"numValue":-0.02964295791055,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526939,"numValue":-0.7660680815807299,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526940,"numValue":1.7321286151696396,"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:19564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,564 | train | mutant | 728,020 | 358 | 728,211 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63H | V28F|V63H | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,849 | MegaScale | null | null | null | null | 1.77725 | null | null | null | null | null | null | -0.116377 | -0.759544 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526941,"numValue":-0.1163771773576948,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526942,"numValue":-0.7595444095428265,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526943,"numValue":1.7772503431110775,"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:19566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,566 | train | mutant | 728,022 | 358 | 728,213 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63R | V28F|V63R | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,851 | MegaScale | null | null | null | null | 1.838827 | null | null | null | null | null | null | -0.375964 | -0.752683 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526947,"numValue":-0.3759641182056771,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526948,"numValue":-0.7526826036381065,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526949,"numValue":1.838827437420369,"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:19567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,567 | train | mutant | 728,023 | 358 | 728,214 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63K | V28F|V63K | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,852 | MegaScale | null | null | null | null | 1.774706 | null | null | null | null | null | null | -0.183476 | -0.7327 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526950,"numValue":-0.183475568311372,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526951,"numValue":-0.732700439637948,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526952,"numValue":1.774705842548688,"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:19568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,568 | train | mutant | 728,024 | 358 | 728,215 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63T | V28F|V63T | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,853 | MegaScale | null | null | null | null | 2.255107 | null | null | null | null | null | null | 0.368941 | -0.401933 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526953,"numValue":0.3689411947091278,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526954,"numValue":-0.40193284432672,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526955,"numValue":2.255107376295882,"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:19569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,569 | train | mutant | 728,025 | 358 | 728,216 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63S | V28F|V63S | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,854 | MegaScale | null | null | null | null | 1.571247 | null | null | null | null | null | null | -0.082789 | -0.921285 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526956,"numValue":-0.0827894096697462,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526957,"numValue":-0.921285349652844,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526958,"numValue":1.5712470687201423,"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:19570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,570 | train | mutant | 728,026 | 358 | 728,217 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63A | V28F|V63A | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,855 | MegaScale | null | null | null | null | 2.813762 | null | null | null | null | null | null | 0.548563 | -0.043307 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526959,"numValue":0.5485626448753729,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526960,"numValue":-0.0433073221434314,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526961,"numValue":2.8137615297289127,"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:19571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,571 | train | mutant | 728,027 | 358 | 728,218 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63G | V28F|V63G | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,856 | MegaScale | null | null | null | null | 1.837845 | null | null | null | null | null | null | 0.014989 | -0.657202 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526962,"numValue":0.014989474809,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526963,"numValue":-0.657202180657792,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526964,"numValue":1.837844521802948,"references":[],"strValue":null,"type":... | [{"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:19572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,572 | train | mutant | 728,028 | 358 | 728,219 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63M | V28F|V63M | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,857 | MegaScale | null | null | null | null | 4.433541 | null | null | null | null | null | null | 1.812971 | 0.923882 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526965,"numValue":1.8129714662802168,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526966,"numValue":0.9238816524360578,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526967,"numValue":4.433541384292395,"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:19573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,573 | train | mutant | 728,029 | 358 | 728,220 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63C | V28F|V63C | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,858 | MegaScale | null | null | null | null | 2.610053 | null | null | null | null | null | null | 0.518099 | -0.176458 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526968,"numValue":0.5180987481786921,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526969,"numValue":-0.1764579579491557,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526970,"numValue":2.6100533922375977,"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:19574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,574 | train | mutant | 728,030 | 358 | 728,221 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63L | V28F|V63L | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,859 | MegaScale | null | null | null | null | 4.481945 | null | null | null | null | null | null | 1.846704 | 0.94879 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526971,"numValue":1.8467036422827507,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526972,"numValue":0.9487899705508432,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526973,"numValue":4.481944707681906,"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:19575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,575 | train | mutant | 728,031 | 358 | 728,222 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63I | V28F|V63I | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,861 | MegaScale | null | null | null | null | 4.545102 | null | null | null | null | null | null | 1.987325 | 1.019591 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526977,"numValue":1.9873247760470985,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526978,"numValue":1.0195907056122506,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526979,"numValue":4.545101859587429,"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:19576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,576 | train | mutant | 728,032 | 358 | 728,223 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63W | V28F|V63W | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,862 | MegaScale | null | null | null | null | 1.074905 | null | null | null | null | null | null | -0.079313 | -1.551257 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526980,"numValue":-0.0793131344600605,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526981,"numValue":-1.5512569206877227,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526982,"numValue":1.074904939864071,"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:19577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,577 | train | mutant | 728,033 | 358 | 728,224 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63Y | V28F|V63Y | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,863 | MegaScale | null | null | null | null | 0.747397 | null | null | null | null | null | null | -0.225444 | -1.832894 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526983,"numValue":-0.225444355333488,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526984,"numValue":-1.8328944285020576,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526985,"numValue":0.7473965691251111,"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:19578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,578 | train | mutant | 728,034 | 358 | 728,225 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63F | V28F|V63F | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,864 | MegaScale | null | null | null | null | 2.1955 | null | null | null | null | null | null | 0.615682 | -0.771416 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526986,"numValue":0.6156823278177395,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526987,"numValue":-0.7714162260262767,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526988,"numValue":2.195499947527032,"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:19579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,579 | train | mutant | 728,035 | 358 | 728,226 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28F|V63P | V28F|V63P | 2 | 2 | 0 | 0 | 28 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,865 | MegaScale | null | null | null | null | 1.906651 | null | null | null | null | null | null | 0.121543 | -0.65412 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526989,"numValue":0.1215434502717419,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526990,"numValue":-0.654119559956183,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526991,"numValue":1.9066511104144797,"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:19580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,580 | train | mutant | 728,036 | 358 | 728,227 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63Q | V28P|V63Q | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,866 | MegaScale | null | null | null | null | -0.200698 | null | null | null | null | null | null | -0.625135 | -1.444658 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526992,"numValue":-0.6251347422397195,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526993,"numValue":-1.4446582029526756,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526994,"numValue":-0.2006981511588416,"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:19582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,582 | train | mutant | 728,038 | 358 | 728,229 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63N | V28P|V63N | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,868 | MegaScale | null | null | null | null | 0.186774 | null | null | null | null | null | null | -0.5427 | -1.317072 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526998,"numValue":-0.5426996322181752,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526999,"numValue":-1.3170715087038598,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527000,"numValue":0.1867739475754782,"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:19583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,583 | train | mutant | 728,039 | 358 | 728,230 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63H | V28P|V63H | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,869 | MegaScale | null | null | null | null | 0.150167 | null | null | null | null | null | null | -0.528891 | -1.382567 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527001,"numValue":-0.5288909355401958,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527002,"numValue":-1.3825667587259614,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527003,"numValue":0.1501666881574387,"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:19584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,584 | train | mutant | 728,040 | 358 | 728,231 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63D | V28P|V63D | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,870 | MegaScale | null | null | null | null | 0.098687 | null | null | null | null | null | null | -0.481682 | -1.326889 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527004,"numValue":-0.4816820518142665,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527005,"numValue":-1.3268887096668815,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527006,"numValue":0.0986870293315357,"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:19585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,585 | train | mutant | 728,041 | 358 | 728,232 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63R | V28P|V63R | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,871 | MegaScale | null | null | null | null | 0.182909 | null | null | null | null | null | null | -0.843659 | -1.410343 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527007,"numValue":-0.8436591819139698,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527008,"numValue":-1.410343097961099,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527009,"numValue":0.1829093976271886,"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:19586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,586 | train | mutant | 728,042 | 358 | 728,233 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63K | V28P|V63K | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,872 | MegaScale | null | null | null | null | 0.17837 | null | null | null | null | null | null | -0.742093 | -1.334895 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527010,"numValue":-0.7420925794693258,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527011,"numValue":-1.3348948847127249,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527012,"numValue":0.178369858567538,"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:19587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,587 | train | mutant | 728,043 | 358 | 728,234 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63T | V28P|V63T | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,873 | MegaScale | null | null | null | null | 0.145636 | null | null | null | null | null | null | -0.543479 | -1.363761 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527013,"numValue":-0.5434792209253541,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527014,"numValue":-1.36376060404364,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527015,"numValue":0.1456360127667977,"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:19588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,588 | train | mutant | 728,044 | 358 | 728,235 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63S | V28P|V63S | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,874 | MegaScale | null | null | null | null | 0.139067 | null | null | null | null | null | null | -0.523659 | -1.364558 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527016,"numValue":-0.5236588168842246,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527017,"numValue":-1.364557644062921,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527018,"numValue":0.1390674585357126,"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:19589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,589 | train | mutant | 728,045 | 358 | 728,236 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63A | V28P|V63A | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,875 | MegaScale | null | null | null | null | 0.064357 | null | null | null | null | null | null | -0.593594 | -1.357377 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527019,"numValue":-0.5935937399451312,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527020,"numValue":-1.3573768966895698,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527021,"numValue":0.0643572100696994,"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:19590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,590 | train | mutant | 728,046 | 358 | 728,237 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63G | V28P|V63G | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,876 | MegaScale | null | null | null | null | 0.180766 | null | null | null | null | null | null | -0.584757 | -1.281961 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527022,"numValue":-0.5847574411963504,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527023,"numValue":-1.2819610220823248,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527024,"numValue":0.1807662070051909,"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:19591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,591 | train | mutant | 728,047 | 358 | 728,238 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63M | V28P|V63M | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,877 | MegaScale | null | null | null | null | 0.285484 | null | null | null | null | null | null | -0.639424 | -1.342239 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527025,"numValue":-0.6394241837014529,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527026,"numValue":-1.3422387085519794,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527027,"numValue":0.2854843028300308,"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:19592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,592 | train | mutant | 728,048 | 358 | 728,239 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63C | V28P|V63C | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,878 | MegaScale | null | null | null | null | 0.314958 | null | null | null | null | null | null | -0.521284 | -1.297051 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527028,"numValue":-0.5212843097855564,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527029,"numValue":-1.2970513490999451,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527030,"numValue":0.3149575469287367,"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:19593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,593 | train | mutant | 728,049 | 358 | 728,240 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63L | V28P|V63L | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,879 | MegaScale | null | null | null | null | 0.272741 | null | null | null | null | null | null | -0.667497 | -1.360306 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527031,"numValue":-0.667497361808763,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527032,"numValue":-1.3603064439412869,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527033,"numValue":0.2727414758997748,"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:19594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,594 | train | mutant | 728,050 | 358 | 728,241 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63I | V28P|V63I | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,881 | MegaScale | null | null | null | null | 0.027097 | null | null | null | null | null | null | -0.609939 | -1.380932 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527037,"numValue":-0.6099385101831756,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527038,"numValue":-1.380932271273283,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527039,"numValue":0.0270972307367735,"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:19595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,595 | train | mutant | 728,051 | 358 | 728,242 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63W | V28P|V63W | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,882 | MegaScale | null | null | null | null | 0.077432 | null | null | null | null | null | null | -0.652923 | -1.887146 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527040,"numValue":-0.6529226986601837,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527041,"numValue":-1.8871458168603616,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527042,"numValue":0.0774323225328602,"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:19596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,596 | train | mutant | 728,052 | 358 | 728,243 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63Y | V28P|V63Y | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,883 | MegaScale | null | null | null | null | -0.417742 | null | null | null | null | null | null | -0.751765 | -1.985285 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527043,"numValue":-0.7517649636407686,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527044,"numValue":-1.9852853894830544,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527045,"numValue":-0.4177419158426111,"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:19597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,597 | train | mutant | 728,053 | 358 | 728,244 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63F | V28P|V63F | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,884 | MegaScale | null | null | null | null | 0.100474 | null | null | null | null | null | null | -0.771022 | -1.678759 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527046,"numValue":-0.7710223150628384,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527047,"numValue":-1.6787589143124813,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527048,"numValue":0.1004736786443642,"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:19598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,598 | train | mutant | 728,054 | 358 | 728,245 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28P|V63P | V28P|V63P | 2 | 2 | 0 | 0 | 28 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,885 | MegaScale | null | null | null | null | 0.207194 | null | null | null | null | null | null | -0.457338 | -1.301336 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3527049,"numValue":-0.4573379031421758,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3527050,"numValue":-1.3013355497367534,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3527051,"numValue":0.2071940640495675,"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:19599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,599 | train | mutant | 476,322 | 358 | 477,674 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29Q | H29Q | 1 | 1 | 0 | 0 | 29 | H | Q | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,956 | MegaScale | null | null | null | null | 3.961638 | null | null | null | null | null | null | 1.704327 | 0.795012 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365752,"numValue":1.704326841361821,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365753,"numValue":0.7950115032680789,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365754,"numValue":3.961637927924256,"references":[],"strValue":null,"typ... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,600 | train | mutant | 476,322 | 358 | 477,674 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29Q | H29Q | 1 | 1 | 0 | 0 | 29 | H | Q | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,310 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.337354 | 0.049842 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123302,"numValue":-0.337353983672509,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123303,"numValue":0.0498415135066042,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,601 | train | mutant | 476,323 | 358 | 477,675 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29E | H29E | 1 | 1 | 0 | 0 | 29 | H | E | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,957 | MegaScale | null | null | null | null | 3.370457 | null | null | null | null | null | null | 1.390932 | 0.530089 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365755,"numValue":1.390932492755088,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365756,"numValue":0.5300893692172457,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365757,"numValue":3.3704574117677897,"references":[],"strValue":null,"ty... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,602 | train | mutant | 476,323 | 358 | 477,675 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29E | H29E | 1 | 1 | 0 | 0 | 29 | H | E | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,064,542 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.130521 | 0.044539 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12121766,"numValue":-0.130521427586126,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121767,"numValue":0.044539246498678,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,603 | train | mutant | 476,324 | 358 | 477,676 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29N | H29N | 1 | 1 | 0 | 0 | 29 | H | N | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,958 | MegaScale | null | null | null | null | 4.109212 | null | null | null | null | null | null | 1.727107 | 0.856454 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365758,"numValue":1.727107239702548,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365759,"numValue":0.8564543937300134,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365760,"numValue":4.109211936297927,"references":[],"strValue":null,"typ... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,605 | train | mutant | 476,325 | 358 | 477,677 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29D | H29D | 1 | 1 | 0 | 0 | 29 | H | D | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,959 | MegaScale | null | null | null | null | 3.392225 | null | null | null | null | null | null | 1.494698 | 0.695663 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365761,"numValue":1.4946975418615582,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365762,"numValue":0.6956631183687279,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365763,"numValue":3.3922251774505456,"references":[],"strValue":null,"t... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,607 | train | mutant | 476,326 | 358 | 477,678 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29R | H29R | 1 | 1 | 0 | 0 | 29 | H | R | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,960 | MegaScale | null | null | null | null | 4.210745 | null | null | null | null | null | null | 1.781626 | 0.816157 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365764,"numValue":1.7816262625695574,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365765,"numValue":0.8161572555640783,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365766,"numValue":4.2107451626592685,"references":[],"strValue":null,"t... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,608 | train | mutant | 476,326 | 358 | 477,678 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29R | H29R | 1 | 1 | 0 | 0 | 29 | H | R | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,311 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.277825 | 0.037227 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123304,"numValue":-0.277824716066628,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123305,"numValue":0.0372266154756837,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,609 | train | mutant | 476,327 | 358 | 477,679 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29K | H29K | 1 | 1 | 0 | 0 | 29 | H | K | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,961 | MegaScale | null | null | null | null | 3.348504 | null | null | null | null | null | null | 1.168599 | 0.372864 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365767,"numValue":1.1685986895772038,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365768,"numValue":0.372863815244667,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365769,"numValue":3.348503786428841,"references":[],"strValue":null,"typ... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,610 | train | mutant | 476,327 | 358 | 477,679 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29K | H29K | 1 | 1 | 0 | 0 | 29 | H | K | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,305 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.259213 | 0.045238 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123292,"numValue":-0.259213233044116,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123293,"numValue":0.0452376677917749,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,611 | train | mutant | 476,328 | 358 | 477,680 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29T | H29T | 1 | 1 | 0 | 0 | 29 | H | T | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,962 | MegaScale | null | null | null | null | 4.160642 | null | null | null | null | null | null | 1.810177 | 0.847839 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365770,"numValue":1.8101774635410617,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365771,"numValue":0.8478389472492901,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365772,"numValue":4.160641925467813,"references":[],"strValue":null,"ty... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,612 | train | mutant | 476,328 | 358 | 477,680 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29T | H29T | 1 | 1 | 0 | 0 | 29 | H | T | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,313 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.300877 | 0.054375 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123308,"numValue":-0.300876850851694,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123309,"numValue":0.0543750386793649,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,613 | train | mutant | 476,329 | 358 | 477,681 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29S | H29S | 1 | 1 | 0 | 0 | 29 | H | S | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,963 | MegaScale | null | null | null | null | 4.176326 | null | null | null | null | null | null | 1.861476 | 0.845618 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365773,"numValue":1.861475675907459,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365774,"numValue":0.8456177163323895,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365775,"numValue":4.176326402547369,"references":[],"strValue":null,"typ... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,614 | train | mutant | 476,329 | 358 | 477,681 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29S | H29S | 1 | 1 | 0 | 0 | 29 | H | S | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,312 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.242077 | 0.04018 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123306,"numValue":-0.242076856028366,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123307,"numValue":0.0401798267691934,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,615 | train | mutant | 476,330 | 358 | 477,682 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29A | H29A | 1 | 1 | 0 | 0 | 29 | H | A | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,964 | MegaScale | null | null | null | null | 3.828871 | null | null | null | null | null | null | 1.652881 | 0.611247 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365776,"numValue":1.6528812631647731,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365777,"numValue":0.6112472193197901,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365778,"numValue":3.8288706109687567,"references":[],"strValue":null,"t... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,616 | train | mutant | 476,330 | 358 | 477,682 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29A | H29A | 1 | 1 | 0 | 0 | 29 | H | A | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,064,539 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.472879 | 0.038998 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12121760,"numValue":-0.47287924070743,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121761,"numValue":0.0389980000506627,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,617 | train | mutant | 476,331 | 358 | 477,683 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29G | H29G | 1 | 1 | 0 | 0 | 29 | H | G | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,965 | MegaScale | null | null | null | null | 3.658509 | null | null | null | null | null | null | 1.574665 | 0.619867 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365779,"numValue":1.57466548418881,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365780,"numValue":0.6198672126925604,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365781,"numValue":3.658508729857033,"references":[],"strValue":null,"type... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,618 | train | mutant | 476,331 | 358 | 477,683 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29G | H29G | 1 | 1 | 0 | 0 | 29 | H | G | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,064,544 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.416931 | 0.045054 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12121770,"numValue":-0.41693058592744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121771,"numValue":0.0450535463480454,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,619 | train | mutant | 476,332 | 358 | 477,684 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29M | H29M | 1 | 1 | 0 | 0 | 29 | H | M | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,966 | MegaScale | null | null | null | null | 4.901031 | null | null | null | null | null | null | 2.221328 | 1.24168 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365782,"numValue":2.2213281212874074,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365783,"numValue":1.2416796855772647,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365784,"numValue":4.901031272214187,"references":[],"strValue":null,"ty... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,620 | train | mutant | 476,332 | 358 | 477,684 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29M | H29M | 1 | 1 | 0 | 0 | 29 | H | M | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,307 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.71842 | 0.056008 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123296,"numValue":-0.718420173120404,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123297,"numValue":0.0560081803674983,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,621 | train | mutant | 476,333 | 358 | 477,685 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29L | H29L | 1 | 1 | 0 | 0 | 29 | H | L | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,967 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.195545 | 1.333657 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365785,"numValue":2.1955451816041083,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365786,"numValue":1.333656968094453,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365787,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,622 | train | mutant | 476,333 | 358 | 477,685 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29L | H29L | 1 | 1 | 0 | 0 | 29 | H | L | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,306 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.80258 | 0.044453 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123294,"numValue":-0.802579540261286,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123295,"numValue":0.0444527825927432,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,623 | train | mutant | 476,334 | 358 | 477,686 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29V | H29V | 1 | 1 | 0 | 0 | 29 | H | V | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,968 | MegaScale | null | null | null | null | 4.017869 | null | null | null | null | null | null | 1.687861 | 0.736705 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365788,"numValue":1.6878613275100744,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365789,"numValue":0.7367052975191726,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365790,"numValue":4.017868882670141,"references":[],"strValue":null,"ty... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,624 | train | mutant | 476,334 | 358 | 477,686 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29V | H29V | 1 | 1 | 0 | 0 | 29 | H | V | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,314 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.871089 | 0.067571 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123310,"numValue":-0.871089412707244,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123311,"numValue":0.0675714474187884,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,625 | train | mutant | 476,335 | 358 | 477,687 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29I | H29I | 1 | 1 | 0 | 0 | 29 | H | I | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,969 | MegaScale | null | null | null | null | 4.698034 | null | null | null | null | null | null | 1.999099 | 1.158015 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365791,"numValue":1.9990990641588249,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365792,"numValue":1.1580148968152866,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365793,"numValue":4.6980340866451655,"references":[],"strValue":null,"t... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,626 | train | mutant | 476,335 | 358 | 477,687 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29I | H29I | 1 | 1 | 0 | 0 | 29 | H | I | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,304 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.811875 | 0.149912 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123290,"numValue":-0.811875468177486,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123291,"numValue":0.149911926051127,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,627 | train | mutant | 476,336 | 358 | 477,688 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29W | H29W | 1 | 1 | 0 | 0 | 29 | H | W | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,970 | MegaScale | null | null | null | null | 4.863316 | null | null | null | null | null | null | 2.156097 | 1.161109 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365794,"numValue":2.1560973885374417,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365795,"numValue":1.1611093984922274,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365796,"numValue":4.863316177043423,"references":[],"strValue":null,"ty... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,628 | train | mutant | 476,336 | 358 | 477,688 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29W | H29W | 1 | 1 | 0 | 0 | 29 | H | W | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 5,065,315 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.753508 | 0.074155 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12123312,"numValue":-0.753508252896099,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123313,"numValue":0.0741545296518695,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,629 | train | mutant | 476,337 | 358 | 477,689 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | H29Y | H29Y | 1 | 1 | 0 | 0 | 29 | H | Y | 9 | CONSERVATION | 1CSP | 247 | null | 29 | A | E | true | false | 61.603778 | 12.009 | 501,971 | MegaScale | null | null | null | null | 4.840993 | null | null | null | null | null | null | 2.059006 | 1.162338 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365797,"numValue":2.059006416792301,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365798,"numValue":1.1623384246048711,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365799,"numValue":4.840992857364254,"references":[],"strValue":null,"typ... | [{"id":20837,"numValue":9.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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