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:19411 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,411 | train | mutant | 727,867 | 358 | 728,058 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63N | V28A|V63N | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,669 | MegaScale | null | null | null | null | -0.164748 | null | null | null | null | null | null | -0.806192 | -1.890188 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526401,"numValue":-0.8061924151328036,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526402,"numValue":-1.8901882947751083,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526403,"numValue":-0.1647482222992386,"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:19412 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,412 | train | mutant | 727,868 | 358 | 728,059 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63H | V28A|V63H | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,670 | MegaScale | null | null | null | null | 0.440571 | null | null | null | null | null | null | -0.519944 | -1.645947 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526404,"numValue":-0.5199440966882751,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526405,"numValue":-1.6459474095042048,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526406,"numValue":0.4405710669042975,"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:19413 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,413 | train | mutant | 727,869 | 358 | 728,060 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63D | V28A|V63D | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,671 | MegaScale | null | null | null | null | 0.341483 | null | null | null | null | null | null | -0.614908 | -1.651372 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526407,"numValue":-0.6149081335436583,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526408,"numValue":-1.651371713667982,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526409,"numValue":0.341482773003638,"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:19415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,415 | train | mutant | 727,871 | 358 | 728,062 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63K | V28A|V63K | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,673 | MegaScale | null | null | null | null | 0.466617 | null | null | null | null | null | null | -0.643112 | -1.652843 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526413,"numValue":-0.6431119061417672,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526414,"numValue":-1.6528431885974548,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526415,"numValue":0.4666165901335772,"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:19416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,416 | train | mutant | 727,872 | 358 | 728,063 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63T | V28A|V63T | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,674 | MegaScale | null | null | null | null | 0.638774 | null | null | null | null | null | null | -0.346485 | -1.581958 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526416,"numValue":-0.3464848211248696,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526417,"numValue":-1.5819577018954614,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526418,"numValue":0.6387736639972867,"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:19417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,417 | train | mutant | 727,873 | 358 | 728,064 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63S | V28A|V63S | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,675 | MegaScale | null | null | null | null | 0.108125 | null | null | null | null | null | null | -0.671611 | -1.729745 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526419,"numValue":-0.6716108328166577,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526420,"numValue":-1.7297451276447176,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526421,"numValue":0.10812512903989,"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:19418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,418 | train | mutant | 727,874 | 358 | 728,065 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63A | V28A|V63A | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,676 | MegaScale | null | null | null | null | 0.902803 | null | null | null | null | null | null | -0.24834 | -1.383581 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526422,"numValue":-0.2483399039899318,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526423,"numValue":-1.383581257570056,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526424,"numValue":0.9028034053254969,"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:19419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,419 | train | mutant | 727,875 | 358 | 728,066 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63G | V28A|V63G | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,677 | MegaScale | null | null | null | null | 0.37485 | null | null | null | null | null | null | -0.565978 | -1.668013 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526425,"numValue":-0.5659782405497213,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526426,"numValue":-1.6680125123565697,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526427,"numValue":0.3748502455285145,"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:19420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,420 | train | mutant | 727,876 | 358 | 728,067 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63M | V28A|V63M | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,678 | MegaScale | null | null | null | null | 2.386935 | null | null | null | null | null | null | 0.609863 | -0.430927 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526428,"numValue":0.6098631479112357,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526429,"numValue":-0.4309266194499761,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526430,"numValue":2.386935273472273,"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:19421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,421 | train | mutant | 727,877 | 358 | 728,068 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63C | V28A|V63C | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,679 | MegaScale | null | null | null | null | 1.089131 | null | null | null | null | null | null | -0.155864 | -1.307568 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526431,"numValue":-0.1558644129292071,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526432,"numValue":-1.3075683222461305,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526433,"numValue":1.0891305413315722,"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:19422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,422 | train | mutant | 727,878 | 358 | 728,069 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63L | V28A|V63L | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,680 | MegaScale | null | null | null | null | 3.568258 | null | null | null | null | null | null | 1.245087 | 0.384138 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526434,"numValue":1.2450870799657512,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526435,"numValue":0.3841378939719997,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526436,"numValue":3.5682581525200643,"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:19423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,423 | train | mutant | 727,879 | 358 | 728,070 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63I | V28A|V63I | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,682 | MegaScale | null | null | null | null | 4.324936 | null | null | null | null | null | null | 1.86874 | 0.889505 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526440,"numValue":1.8687395901575403,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526441,"numValue":0.8895049640237671,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526442,"numValue":4.324936016931575,"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:19424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,424 | train | mutant | 727,880 | 358 | 728,071 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63W | V28A|V63W | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,683 | MegaScale | null | null | null | null | 0.197375 | null | null | null | null | null | null | -0.696006 | -2.026547 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526443,"numValue":-0.6960064141695,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526444,"numValue":-2.026546623966861,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526445,"numValue":0.1973749670831181,"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:19425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,425 | train | mutant | 727,881 | 358 | 728,072 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63Y | V28A|V63Y | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,684 | MegaScale | null | null | null | null | 0.37376 | null | null | null | null | null | null | -0.559084 | -1.927526 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526446,"numValue":-0.5590842049898723,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526447,"numValue":-1.9275255622205625,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526448,"numValue":0.3737599666774925,"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:19426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,426 | train | mutant | 727,882 | 358 | 728,073 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63F | V28A|V63F | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,685 | MegaScale | null | null | null | null | 0.318428 | null | null | null | null | null | null | -0.631454 | -1.949629 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526449,"numValue":-0.631453509965075,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526450,"numValue":-1.9496287840718791,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526451,"numValue":0.3184280712644111,"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:19427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,427 | train | mutant | 727,883 | 358 | 728,074 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28A|V63P | V28A|V63P | 2 | 2 | 0 | 0 | 28 | V | A | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,686 | MegaScale | null | null | null | null | 0.370808 | null | null | null | null | null | null | -0.594693 | -1.633764 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526452,"numValue":-0.5946929560084006,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526453,"numValue":-1.6337644390622228,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526454,"numValue":0.3708077541539644,"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:19428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,428 | train | mutant | 727,884 | 358 | 728,075 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63Q | V28G|V63Q | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,687 | MegaScale | null | null | null | null | 0.332618 | null | null | null | null | null | null | -0.698977 | -1.540233 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526455,"numValue":-0.6989773284200529,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526456,"numValue":-1.5402328438155437,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526457,"numValue":0.3326176652495699,"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:19429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,429 | train | mutant | 727,885 | 358 | 728,076 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63E | V28G|V63E | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,688 | MegaScale | null | null | null | null | 0.514436 | null | null | null | null | null | null | -0.460313 | -1.491947 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526458,"numValue":-0.4603134903675055,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526459,"numValue":-1.491947459689162,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526460,"numValue":0.514436369038765,"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:19430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,430 | train | mutant | 727,886 | 358 | 728,077 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63N | V28G|V63N | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,689 | MegaScale | null | null | null | null | 0.341269 | null | null | null | null | null | null | -0.615733 | -1.577257 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526461,"numValue":-0.6157334519373354,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526462,"numValue":-1.57725722021876,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526463,"numValue":0.3412686786535693,"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:19431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,431 | train | mutant | 727,887 | 358 | 728,078 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63H | V28G|V63H | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,690 | MegaScale | null | null | null | null | 0.320867 | null | null | null | null | null | null | -0.662981 | -1.573465 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526464,"numValue":-0.662981291184644,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526465,"numValue":-1.5734652596375795,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526466,"numValue":0.3208672338739435,"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:19432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,432 | train | mutant | 727,888 | 358 | 728,079 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63D | V28G|V63D | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,691 | MegaScale | null | null | null | null | 0.396927 | null | null | null | null | null | null | -0.455677 | -1.555058 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526467,"numValue":-0.4556765816381383,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526468,"numValue":-1.555058107877569,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526469,"numValue":0.3969274271600468,"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:19433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,433 | train | mutant | 727,889 | 358 | 728,080 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63R | V28G|V63R | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,692 | MegaScale | null | null | null | null | 0.282737 | null | null | null | null | null | null | -0.839471 | -1.660113 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526470,"numValue":-0.839471094666022,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526471,"numValue":-1.66011272832264,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526472,"numValue":0.2827373776541039,"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:19434 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,434 | train | mutant | 727,890 | 358 | 728,081 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63K | V28G|V63K | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,693 | MegaScale | null | null | null | null | 0.398616 | null | null | null | null | null | null | -0.662932 | -1.577606 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526473,"numValue":-0.6629318096698051,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526474,"numValue":-1.577606293427152,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526475,"numValue":0.3986164767037721,"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:19435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,435 | train | mutant | 727,891 | 358 | 728,082 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63T | V28G|V63T | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,694 | MegaScale | null | null | null | null | 0.294593 | null | null | null | null | null | null | -0.581862 | -1.6101 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526476,"numValue":-0.5818622626050511,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526477,"numValue":-1.6101003343879077,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526478,"numValue":0.2945932330773602,"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:19436 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,436 | train | mutant | 727,892 | 358 | 728,083 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63S | V28G|V63S | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,695 | MegaScale | null | null | null | null | 0.474194 | null | null | null | null | null | null | -0.467099 | -1.528418 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526479,"numValue":-0.4670993601075808,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526480,"numValue":-1.5284177901509342,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526481,"numValue":0.474194143998616,"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:19437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,437 | train | mutant | 727,893 | 358 | 728,084 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63A | V28G|V63A | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,696 | MegaScale | null | null | null | null | 0.476315 | null | null | null | null | null | null | -0.580107 | -1.468215 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526482,"numValue":-0.5801073924067731,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526483,"numValue":-1.4682149746906763,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526484,"numValue":0.4763150487035052,"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:19438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,438 | train | mutant | 727,894 | 358 | 728,085 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63G | V28G|V63G | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,697 | MegaScale | null | null | null | null | 0.31344 | null | null | null | null | null | null | -0.550766 | -1.55274 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526485,"numValue":-0.5507657394474099,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526486,"numValue":-1.5527403423842392,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526487,"numValue":0.3134397661037859,"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:19439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,439 | train | mutant | 727,895 | 358 | 728,086 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63M | V28G|V63M | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,698 | MegaScale | null | null | null | null | 0.836733 | null | null | null | null | null | null | -0.338324 | -1.44819 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526488,"numValue":-0.3383241303469574,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526489,"numValue":-1.448189921866191,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526490,"numValue":0.8367334840742204,"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:19440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,440 | train | mutant | 727,896 | 358 | 728,087 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63C | V28G|V63C | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,699 | MegaScale | null | null | null | null | 0.692897 | null | null | null | null | null | null | -0.399408 | -1.412334 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526491,"numValue":-0.3994075948988447,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526492,"numValue":-1.41233396457592,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526493,"numValue":0.6928966728796973,"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:19441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,441 | train | mutant | 727,897 | 358 | 728,088 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63L | V28G|V63L | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,700 | MegaScale | null | null | null | null | 0.828181 | null | null | null | null | null | null | -0.394445 | -1.304455 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526494,"numValue":-0.3944446084481176,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526495,"numValue":-1.304455431197888,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526496,"numValue":0.8281807914981891,"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:19442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,442 | train | mutant | 727,898 | 358 | 728,089 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63I | V28G|V63I | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,702 | MegaScale | null | null | null | null | 2.479574 | null | null | null | null | null | null | 0.74836 | -0.209977 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526500,"numValue":0.7483595816617588,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526501,"numValue":-0.2099771051751111,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526502,"numValue":2.479573929094053,"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:19443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,443 | train | mutant | 727,899 | 358 | 728,090 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63W | V28G|V63W | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,703 | MegaScale | null | null | null | null | 0.011031 | null | null | null | null | null | null | -0.754432 | -2.040963 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526503,"numValue":-0.7544322073019922,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526504,"numValue":-2.0409634459598625,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526505,"numValue":0.0110308954182891,"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:19444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,444 | train | mutant | 727,900 | 358 | 728,091 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63Y | V28G|V63Y | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,704 | MegaScale | null | null | null | null | -0.144008 | null | null | null | null | null | null | -0.72998 | -2.122459 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526506,"numValue":-0.7299800957313098,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526507,"numValue":-2.122458977451503,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526508,"numValue":-0.1440079470856622,"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:19445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,445 | train | mutant | 727,901 | 358 | 728,092 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63F | V28G|V63F | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,705 | MegaScale | null | null | null | null | 0.253325 | null | null | null | null | null | null | -0.685939 | -1.879613 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526509,"numValue":-0.6859386787719944,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526510,"numValue":-1.8796130610226736,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526511,"numValue":0.2533246652397962,"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:19446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,446 | train | mutant | 727,902 | 358 | 728,093 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28G|V63P | V28G|V63P | 2 | 2 | 0 | 0 | 28 | V | G | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,706 | MegaScale | null | null | null | null | 0.220745 | null | null | null | null | null | null | -0.547551 | -1.607476 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526512,"numValue":-0.5475507719941586,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526513,"numValue":-1.607475868354367,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526514,"numValue":0.2207450443415343,"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:19447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,447 | train | mutant | 727,903 | 358 | 728,094 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63Q | V28M|V63Q | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,707 | MegaScale | null | null | null | null | 0.865971 | null | null | null | null | null | null | -0.479323 | -1.441142 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526515,"numValue":-0.4793232225395591,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526516,"numValue":-1.441141923156946,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526517,"numValue":0.8659710948957102,"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:19448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,448 | train | mutant | 727,904 | 358 | 728,095 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63E | V28M|V63E | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,708 | MegaScale | null | null | null | null | 0.512332 | null | null | null | null | null | null | -0.467552 | -1.624999 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526518,"numValue":-0.4675516693517346,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526519,"numValue":-1.624999352449103,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526520,"numValue":0.5123321600405195,"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:19450 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,450 | train | mutant | 727,906 | 358 | 728,097 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63H | V28M|V63H | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,710 | MegaScale | null | null | null | null | 0.79374 | null | null | null | null | null | null | -0.451669 | -1.435216 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526524,"numValue":-0.4516692254560174,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526525,"numValue":-1.4352159531993394,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526526,"numValue":0.7937396845470698,"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:19452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,452 | train | mutant | 727,908 | 358 | 728,099 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63R | V28M|V63R | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,712 | MegaScale | null | null | null | null | 0.691218 | null | null | null | null | null | null | -0.747298 | -1.512553 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526530,"numValue":-0.7472981424333816,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526531,"numValue":-1.5125527142577049,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526532,"numValue":0.6912177758096245,"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:19453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,453 | train | mutant | 727,909 | 358 | 728,100 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63K | V28M|V63K | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,713 | MegaScale | null | null | null | null | 0.653558 | null | null | null | null | null | null | -0.509384 | -1.528271 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526533,"numValue":-0.5093840495790165,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526534,"numValue":-1.528270622146382,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526535,"numValue":0.6535584272856393,"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:19455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,455 | train | mutant | 727,911 | 358 | 728,102 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63S | V28M|V63S | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,715 | MegaScale | null | null | null | null | 0.700531 | null | null | null | null | null | null | -0.472634 | -1.527312 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526539,"numValue":-0.4726338913887331,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526540,"numValue":-1.5273115811439848,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526541,"numValue":0.7005312465578926,"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:19457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,457 | train | mutant | 727,913 | 358 | 728,104 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63G | V28M|V63G | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,717 | MegaScale | null | null | null | null | 0.862861 | null | null | null | null | null | null | -0.416224 | -1.34629 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526545,"numValue":-0.4162238051042724,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526546,"numValue":-1.34628987932835,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526547,"numValue":0.8628614225916353,"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:19458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,458 | train | mutant | 727,914 | 358 | 728,105 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63M | V28M|V63M | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,718 | MegaScale | null | null | null | null | 1.928627 | null | null | null | null | null | null | 0.244915 | -0.735074 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526548,"numValue":0.2449153242388032,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526549,"numValue":-0.7350740116916743,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526550,"numValue":1.9286270188050985,"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:19459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,459 | train | mutant | 727,915 | 358 | 728,106 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63C | V28M|V63C | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,719 | MegaScale | null | null | null | null | 1.555518 | null | null | null | null | null | null | 0.233661 | -1.097818 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526551,"numValue":0.2336608082634839,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526552,"numValue":-1.0978181734962242,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526553,"numValue":1.555517737307619,"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:19460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,460 | train | mutant | 727,916 | 358 | 728,107 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63L | V28M|V63L | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,720 | MegaScale | null | null | null | null | 3.118522 | null | null | null | null | null | null | 1.115504 | 0.068214 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526554,"numValue":1.1155041342853318,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526555,"numValue":0.0682141083898226,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526556,"numValue":3.1185215719679817,"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:19461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,461 | train | mutant | 727,917 | 358 | 728,108 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63I | V28M|V63I | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,722 | MegaScale | null | null | null | null | 4.198377 | null | null | null | null | null | null | 1.729652 | 0.810986 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526560,"numValue":1.7296519747191148,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526561,"numValue":0.8109859534336877,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526562,"numValue":4.198376551157532,"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:19462 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,462 | train | mutant | 727,918 | 358 | 728,109 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63W | V28M|V63W | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,723 | MegaScale | null | null | null | null | 0.543986 | null | null | null | null | null | null | -0.451632 | -1.904933 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526563,"numValue":-0.451631763305437,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526564,"numValue":-1.9049334922202608,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526565,"numValue":0.5439860427422333,"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:19463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,463 | train | mutant | 727,919 | 358 | 728,110 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63Y | V28M|V63Y | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,724 | MegaScale | null | null | null | null | 0.544335 | null | null | null | null | null | null | -0.617496 | -1.865813 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526566,"numValue":-0.617495878869242,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526567,"numValue":-1.8658126412064524,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526568,"numValue":0.5443346736292478,"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:19464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,464 | train | mutant | 727,920 | 358 | 728,111 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28M|V63F | V28M|V63F | 2 | 2 | 0 | 0 | 28 | V | M | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,725 | MegaScale | null | null | null | null | 0.764414 | null | null | null | null | null | null | -0.474604 | -1.668594 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526569,"numValue":-0.4746035525174185,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526570,"numValue":-1.668593888691697,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526571,"numValue":0.7644136982743165,"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:19467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,467 | train | mutant | 727,923 | 358 | 728,114 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63E | V28C|V63E | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,728 | MegaScale | null | null | null | null | 1.587506 | null | null | null | null | null | null | 0.027192 | -0.707429 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526578,"numValue":0.0271923765235805,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526579,"numValue":-0.7074289094705788,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526580,"numValue":1.5875063745672398,"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:19468 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,468 | train | mutant | 727,924 | 358 | 728,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63N | V28C|V63N | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,729 | MegaScale | null | null | null | null | 1.678011 | null | null | null | null | null | null | -0.174871 | -0.628398 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526581,"numValue":-0.1748714649855933,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526582,"numValue":-0.6283976570257703,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526583,"numValue":1.6780114296921211,"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:19469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,469 | train | mutant | 727,925 | 358 | 728,116 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63H | V28C|V63H | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,730 | MegaScale | null | null | null | null | 1.666831 | null | null | null | null | null | null | -0.169979 | -0.664344 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526584,"numValue":-0.1699789035401284,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526585,"numValue":-0.664344344561467,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526586,"numValue":1.6668312877515497,"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:19470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,470 | train | mutant | 727,926 | 358 | 728,117 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63D | V28C|V63D | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,731 | MegaScale | null | null | null | null | 1.545683 | null | null | null | null | null | null | 0.049393 | -0.74054 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526587,"numValue":0.0493925269967581,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526588,"numValue":-0.7405398795603053,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526589,"numValue":1.545682651193104,"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:19471 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,471 | train | mutant | 727,927 | 358 | 728,118 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63R | V28C|V63R | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,732 | MegaScale | null | null | null | null | 1.402114 | null | null | null | null | null | null | -0.274421 | -0.876399 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526590,"numValue":-0.2744208870536924,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526591,"numValue":-0.8763993529688265,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526592,"numValue":1.4021138792423449,"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:19472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,472 | train | mutant | 727,928 | 358 | 728,119 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63K | V28C|V63K | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,733 | MegaScale | null | null | null | null | 1.629375 | null | null | null | null | null | null | -0.314699 | -0.775672 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526593,"numValue":-0.3146985527135751,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526594,"numValue":-0.7756722022968503,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526595,"numValue":1.6293746378565026,"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:19473 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,473 | train | mutant | 727,929 | 358 | 728,120 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63T | V28C|V63T | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,734 | MegaScale | null | null | null | null | 1.502679 | null | null | null | null | null | null | -0.176696 | -0.852279 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526596,"numValue":-0.1766962804482713,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526597,"numValue":-0.8522787234213975,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526598,"numValue":1.5026793525504032,"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:19474 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,474 | train | mutant | 727,930 | 358 | 728,121 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63S | V28C|V63S | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,735 | MegaScale | null | null | null | null | 1.577888 | null | null | null | null | null | null | -0.109874 | -0.716562 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526599,"numValue":-0.1098736665334424,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526600,"numValue":-0.7165618153527928,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526601,"numValue":1.577887615718732,"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:19475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,475 | train | mutant | 727,931 | 358 | 728,122 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63A | V28C|V63A | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,736 | MegaScale | null | null | null | null | 1.930531 | null | null | null | null | null | null | 0.188834 | -0.553015 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526602,"numValue":0.1888344914102622,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526603,"numValue":-0.553014621148195,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526604,"numValue":1.9305305630754064,"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:19476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,476 | train | mutant | 727,932 | 358 | 728,123 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63G | V28C|V63G | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,737 | MegaScale | null | null | null | null | 1.670442 | null | null | null | null | null | null | -0.026385 | -0.654912 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526605,"numValue":-0.0263848376401466,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526606,"numValue":-0.6549121891700109,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526607,"numValue":1.6704422700280293,"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:19477 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,477 | train | mutant | 727,933 | 358 | 728,124 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63M | V28C|V63M | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,738 | MegaScale | null | null | null | null | 2.26185 | null | null | null | null | null | null | 0.632551 | -0.565936 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526608,"numValue":0.6325506163192627,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526609,"numValue":-0.5659357512162064,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526610,"numValue":2.2618502021542923,"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:19478 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,478 | train | mutant | 727,934 | 358 | 728,125 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63C | V28C|V63C | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,739 | MegaScale | null | null | null | null | 1.751203 | null | null | null | null | null | null | 0.051596 | -0.770846 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526611,"numValue":0.051596107630701,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526612,"numValue":-0.7708460633614651,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526613,"numValue":1.7512030992722385,"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:19479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,479 | train | mutant | 727,935 | 358 | 728,126 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63L | V28C|V63L | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,740 | MegaScale | null | null | null | null | 4.299568 | null | null | null | null | null | null | 1.832062 | 0.829457 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526614,"numValue":1.832062327097297,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526615,"numValue":0.8294570828815464,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526616,"numValue":4.29956797860406,"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:19480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,480 | train | mutant | 727,936 | 358 | 728,127 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63I | V28C|V63I | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,742 | MegaScale | null | null | null | null | 4.38442 | null | null | null | null | null | null | 1.867332 | 0.993405 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526620,"numValue":1.8673324975465904,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526621,"numValue":0.9934048123047576,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526622,"numValue":4.384420296108297,"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:19482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,482 | train | mutant | 727,938 | 358 | 728,129 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63Y | V28C|V63Y | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,744 | MegaScale | null | null | null | null | 0.701214 | null | null | null | null | null | null | -0.362252 | -1.760206 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526626,"numValue":-0.3622519583084327,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526627,"numValue":-1.760206023219998,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526628,"numValue":0.7012142375830359,"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:19483 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,483 | train | mutant | 727,939 | 358 | 728,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63F | V28C|V63F | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,745 | MegaScale | null | null | null | null | 0.756794 | null | null | null | null | null | null | -0.418268 | -1.645732 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526629,"numValue":-0.4182681342364132,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526630,"numValue":-1.6457317030282663,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526631,"numValue":0.756794468319816,"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:19484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,484 | train | mutant | 727,940 | 358 | 728,131 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28C|V63P | V28C|V63P | 2 | 2 | 0 | 0 | 28 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,746 | MegaScale | null | null | null | null | 2.137373 | null | null | null | null | null | null | 0.375213 | -0.435422 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526632,"numValue":0.3752125479385362,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526633,"numValue":-0.4354217418548934,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526634,"numValue":2.137372820875658,"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:19485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,485 | train | mutant | 727,941 | 358 | 728,132 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63Q | V28L|V63Q | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,747 | MegaScale | null | null | null | null | 0.882033 | null | null | null | null | null | null | -0.411229 | -1.331858 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526635,"numValue":-0.4112289452230661,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526636,"numValue":-1.3318577676092618,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526637,"numValue":0.882033177221934,"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:19486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,486 | train | mutant | 727,942 | 358 | 728,133 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63E | V28L|V63E | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,748 | MegaScale | null | null | null | null | 0.795847 | null | null | null | null | null | null | -0.356021 | -1.294518 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526638,"numValue":-0.3560211619660116,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526639,"numValue":-1.29451772982911,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526640,"numValue":0.7958468715843741,"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:19487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,487 | train | mutant | 727,943 | 358 | 728,134 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63N | V28L|V63N | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,749 | MegaScale | null | null | null | null | 0.928875 | null | null | null | null | null | null | -0.444949 | -1.21156 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526641,"numValue":-0.4449491560841293,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526642,"numValue":-1.2115595788220874,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526643,"numValue":0.9288750371336524,"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:19488 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,488 | train | mutant | 727,944 | 358 | 728,135 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63H | V28L|V63H | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,750 | MegaScale | null | null | null | null | 0.802288 | null | null | null | null | null | null | -0.384893 | -1.395632 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526644,"numValue":-0.3848926410839256,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526645,"numValue":-1.3956324356833472,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526646,"numValue":0.8022875907779681,"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:19489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,489 | train | mutant | 727,945 | 358 | 728,136 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63D | V28L|V63D | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,751 | MegaScale | null | null | null | null | 0.776144 | null | null | null | null | null | null | -0.472833 | -1.311163 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526647,"numValue":-0.4728326538714565,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526648,"numValue":-1.3111629077012108,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526649,"numValue":0.7761438896625455,"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:19490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,490 | train | mutant | 727,946 | 358 | 728,137 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63R | V28L|V63R | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,752 | MegaScale | null | null | null | null | 1.096369 | null | null | null | null | null | null | -0.603678 | -1.185245 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526650,"numValue":-0.6036784431708857,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526651,"numValue":-1.1852447117167642,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526652,"numValue":1.0963686988994614,"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:19491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,491 | train | mutant | 727,947 | 358 | 728,138 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63K | V28L|V63K | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,753 | MegaScale | null | null | null | null | 0.882452 | null | null | null | null | null | null | -0.444911 | -1.282889 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526653,"numValue":-0.4449113534015074,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526654,"numValue":-1.2828887928746615,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526655,"numValue":0.8824522704346305,"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:19493 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,493 | train | mutant | 727,949 | 358 | 728,140 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63S | V28L|V63S | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,755 | MegaScale | null | null | null | null | 1.010416 | null | null | null | null | null | null | -0.337227 | -1.208575 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526659,"numValue":-0.3372266792695539,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526660,"numValue":-1.2085749687267722,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526661,"numValue":1.0104164660799169,"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:19494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,494 | train | mutant | 727,950 | 358 | 728,141 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63A | V28L|V63A | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,756 | MegaScale | null | null | null | null | 2.942868 | null | null | null | null | null | null | 1.014165 | 0.057382 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526662,"numValue":1.0141654825329152,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526663,"numValue":0.0573817749551097,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526664,"numValue":2.942868357189764,"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:19495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,495 | train | mutant | 727,951 | 358 | 728,142 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63G | V28L|V63G | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,757 | MegaScale | null | null | null | null | 0.931796 | null | null | null | null | null | null | -0.317133 | -1.235967 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526665,"numValue":-0.3171334987036299,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526666,"numValue":-1.2359669727499418,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526667,"numValue":0.9317956871326109,"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:19496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,496 | train | mutant | 727,952 | 358 | 728,143 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63M | V28L|V63M | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,758 | MegaScale | null | null | null | null | 2.492714 | null | null | null | null | null | null | 0.499813 | -0.282407 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526668,"numValue":0.4998131044385114,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526669,"numValue":-0.2824068601743928,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526670,"numValue":2.4927137057212403,"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:19497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,497 | train | mutant | 727,953 | 358 | 728,144 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63C | V28L|V63C | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,759 | MegaScale | null | null | null | null | 3.542372 | null | null | null | null | null | null | 1.354326 | 0.412714 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526671,"numValue":1.354326203791567,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526672,"numValue":0.412713545010814,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526673,"numValue":3.542371726807631,"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:19498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,498 | train | mutant | 727,954 | 358 | 728,145 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63L | V28L|V63L | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,760 | MegaScale | null | null | null | null | 3.711962 | null | null | null | null | null | null | 1.453742 | 0.54205 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526674,"numValue":1.4537421931838832,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526675,"numValue":0.5420499197663792,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526676,"numValue":3.711962080741595,"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:19499 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,499 | train | mutant | 727,955 | 358 | 728,146 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63I | V28L|V63I | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,762 | MegaScale | null | null | null | null | 3.968265 | null | null | null | null | null | null | 1.648438 | 0.72707 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526680,"numValue":1.6484384813354065,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526681,"numValue":0.7270701747148032,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526682,"numValue":3.9682650408976414,"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:19500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,500 | train | mutant | 727,956 | 358 | 728,147 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63W | V28L|V63W | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,763 | MegaScale | null | null | null | null | 0.554256 | null | null | null | null | null | null | -0.527776 | -1.795697 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526683,"numValue":-0.527776050957911,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526684,"numValue":-1.7956972173700023,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526685,"numValue":0.5542563125140109,"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:19501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,501 | train | mutant | 727,957 | 358 | 728,148 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63Y | V28L|V63Y | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,764 | MegaScale | null | null | null | null | 0.6804 | null | null | null | null | null | null | -0.449608 | -1.720596 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526686,"numValue":-0.4496076278935955,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526687,"numValue":-1.7205955427606754,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526688,"numValue":0.6804001554966914,"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:19502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,502 | train | mutant | 727,958 | 358 | 728,149 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63F | V28L|V63F | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,765 | MegaScale | null | null | null | null | 1.156074 | null | null | null | null | null | null | -0.238904 | -1.332213 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526689,"numValue":-0.2389035969218914,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526690,"numValue":-1.3322126046241975,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526691,"numValue":1.1560735118506793,"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:19503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,503 | train | mutant | 727,959 | 358 | 728,150 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V28L|V63P | V28L|V63P | 2 | 2 | 0 | 0 | 28 | V | L | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,766 | MegaScale | null | null | null | null | 1.271623 | null | null | null | null | null | null | -0.026764 | -1.073527 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526692,"numValue":-0.0267644686298686,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526693,"numValue":-1.0735265332610395,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526694,"numValue":1.2716230600436949,"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:19504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,504 | train | mutant | 727,960 | 358 | 728,151 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Q | V28I|V63Q | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,786 | MegaScale | null | null | null | null | 1.286522 | null | null | null | null | null | null | -0.18966 | -1.014872 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526752,"numValue":-0.1896604733198524,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526753,"numValue":-1.0148718239119003,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526754,"numValue":1.2865218131257528,"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:19505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,505 | train | mutant | 727,961 | 358 | 728,152 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63E | V28I|V63E | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,787 | MegaScale | null | null | null | null | 1.110541 | null | null | null | null | null | null | -0.205658 | -1.113898 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526755,"numValue":-0.2056579206883103,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526756,"numValue":-1.1138976505294078,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526757,"numValue":1.110541480626251,"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:19506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,506 | train | mutant | 727,962 | 358 | 728,153 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63N | V28I|V63N | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,788 | MegaScale | null | null | null | null | 1.284095 | null | null | null | null | null | null | -0.035864 | -1.086951 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526758,"numValue":-0.0358641980277814,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526759,"numValue":-1.0869507202401083,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526760,"numValue":1.284094775290868,"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:19507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,507 | train | mutant | 727,963 | 358 | 728,154 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63H | V28I|V63H | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,789 | MegaScale | null | null | null | null | 1.219174 | null | null | null | null | null | null | -0.251169 | -1.122246 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526761,"numValue":-0.2511690727119703,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526762,"numValue":-1.1222463934546256,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526763,"numValue":1.2191741316482418,"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:19508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,508 | train | mutant | 727,964 | 358 | 728,155 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63D | V28I|V63D | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,790 | MegaScale | null | null | null | null | 1.112622 | null | null | null | null | null | null | -0.051617 | -1.226172 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526764,"numValue":-0.0516174195896756,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526765,"numValue":-1.2261720978905604,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526766,"numValue":1.1126219868627234,"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:19509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,509 | train | mutant | 727,965 | 358 | 728,156 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63R | V28I|V63R | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,791 | MegaScale | null | null | null | null | 1.160683 | null | null | null | null | null | null | -0.830442 | -1.099976 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526767,"numValue":-0.8304424173355747,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526768,"numValue":-1.0999759255524006,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526769,"numValue":1.1606828221178622,"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:19510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,510 | train | mutant | 727,966 | 358 | 728,157 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63K | V28I|V63K | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,792 | MegaScale | null | null | null | null | 1.112565 | null | null | null | null | null | null | -0.4252 | -1.147659 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526770,"numValue":-0.4252002544479221,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526771,"numValue":-1.1476588642900998,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526772,"numValue":1.1125647081688228,"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:19511 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,511 | train | mutant | 727,967 | 358 | 728,158 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63T | V28I|V63T | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,793 | MegaScale | null | null | null | null | 3.595114 | null | null | null | null | null | null | 1.429174 | 0.476515 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526773,"numValue":1.429174318148318,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526774,"numValue":0.4765147166191004,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526775,"numValue":3.5951144778104,"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:19512 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,512 | train | mutant | 727,968 | 358 | 728,159 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63S | V28I|V63S | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,794 | MegaScale | null | null | null | null | 1.98733 | null | null | null | null | null | null | 0.421637 | -0.589988 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526776,"numValue":0.4216371071771325,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526777,"numValue":-0.5899876452188472,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526778,"numValue":1.987330303326588,"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:19514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,514 | train | mutant | 727,970 | 358 | 728,161 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63G | V28I|V63G | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,796 | MegaScale | null | null | null | null | 2.101856 | null | null | null | null | null | null | 0.531876 | -0.526557 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526782,"numValue":0.5318756224943959,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526783,"numValue":-0.5265574755002893,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526784,"numValue":2.1018559689692378,"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:19515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,515 | train | mutant | 727,971 | 358 | 728,162 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63M | V28I|V63M | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,797 | MegaScale | null | null | null | null | 3.559193 | null | null | null | null | null | null | 1.323832 | 0.434922 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526785,"numValue":1.3238321594601064,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526786,"numValue":0.4349219698899146,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526787,"numValue":3.559193094576941,"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:19516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,516 | train | mutant | 727,972 | 358 | 728,163 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63C | V28I|V63C | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,798 | MegaScale | null | null | null | null | 4.389536 | null | null | null | null | null | null | 1.828536 | 0.9407 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526788,"numValue":1.8285363852084364,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526789,"numValue":0.9407004415302422,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526790,"numValue":4.389535707949134,"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:19517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,517 | train | mutant | 727,973 | 358 | 728,164 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63L | V28I|V63L | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,799 | MegaScale | null | null | null | null | 4.398577 | null | null | null | null | null | null | 1.8065 | 0.962626 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526791,"numValue":1.806500132703461,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526792,"numValue":0.962626483999396,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526793,"numValue":4.398577228337854,"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:19518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,518 | train | mutant | 727,974 | 358 | 728,165 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63I | V28I|V63I | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,801 | MegaScale | null | null | null | null | 3.845811 | null | null | null | null | null | null | 1.577006 | 0.629999 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526797,"numValue":1.5770061676475269,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526798,"numValue":0.6299994754742428,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526799,"numValue":3.845810549437835,"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:19519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,519 | train | mutant | 727,975 | 358 | 728,166 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63W | V28I|V63W | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,802 | MegaScale | null | null | null | null | 0.671914 | null | null | null | null | null | null | -0.396199 | -1.795389 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526800,"numValue":-0.3961992832963585,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526801,"numValue":-1.7953887912993447,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526802,"numValue":0.6719137011572631,"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:19520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,520 | train | mutant | 727,976 | 358 | 728,167 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|V63Y | V28I|V63Y | 2 | 2 | 0 | 0 | 28 | V | I | 9 | CONSERVATION | 1CSP | 247 | null | 28|63 | A | E | false | false | 0 | 16.637143 | 778,803 | MegaScale | null | null | null | null | 0.606947 | null | null | null | null | null | null | -0.420041 | -1.778536 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":3526803,"numValue":-0.4200409289858984,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":3526804,"numValue":-1.7785355490391486,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":3526805,"numValue":0.6069468912400473,"references":[],"strValue":null,... | [{"id":20836,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20871,"numValue":9.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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