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:20623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,623 | train | mutant | 476,747 | 358 | 286,814 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49R | F49R | 1 | 1 | 0 | 0 | 49 | F | R | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,082 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.795476 | 0.041763 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122846,"numValue":-0.795475969480455,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122847,"numValue":0.0417628393870846,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,624 | train | mutant | 476,748 | 358 | 286,815 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49K | F49K | 1 | 1 | 0 | 0 | 49 | F | K | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,402 | MegaScale | null | null | null | null | 0.288835 | null | null | null | null | null | null | -0.541108 | -1.645704 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367089,"numValue":-0.541108354937236,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367090,"numValue":-1.6457037233151612,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367091,"numValue":0.2888350648530775,"references":[],"strValue":null,"... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,625 | train | mutant | 476,748 | 358 | 286,815 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49K | F49K | 1 | 1 | 0 | 0 | 49 | F | K | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,076 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.519032 | 0.072731 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122834,"numValue":-0.519032148908057,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122835,"numValue":0.0727309450191497,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,626 | train | mutant | 476,749 | 358 | 286,816 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49T | F49T | 1 | 1 | 0 | 0 | 49 | F | T | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,403 | MegaScale | null | null | null | null | 2.250182 | null | null | null | null | null | null | 0.594898 | -0.36589 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367092,"numValue":0.594897930247663,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367093,"numValue":-0.3658895876910551,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367094,"numValue":2.2501816466302893,"references":[],"strValue":null,"t... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,628 | train | mutant | 476,750 | 358 | 286,817 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49S | F49S | 1 | 1 | 0 | 0 | 49 | F | S | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,404 | MegaScale | null | null | null | null | 0.695107 | null | null | null | null | null | null | -0.198371 | -1.415065 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367095,"numValue":-0.1983714244898276,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367096,"numValue":-1.415065370628985,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367097,"numValue":0.6951070187710733,"references":[],"strValue":null,"... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,629 | train | mutant | 476,750 | 358 | 286,817 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49S | F49S | 1 | 1 | 0 | 0 | 49 | F | S | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,083 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.791644 | 0.056663 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122848,"numValue":-0.791643576606426,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122849,"numValue":0.0566633789078732,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,630 | train | mutant | 476,751 | 358 | 285,767 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49A | F49A | 1 | 1 | 0 | 0 | 49 | F | A | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,405 | MegaScale | null | null | null | null | 2.241747 | null | null | null | null | null | null | 0.623312 | -0.374995 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367098,"numValue":0.62331193030597,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367099,"numValue":-0.3749951904824343,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367100,"numValue":2.2417466617452364,"references":[],"strValue":null,"ty... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,631 | train | mutant | 476,751 | 358 | 285,767 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49A | F49A | 1 | 1 | 0 | 0 | 49 | F | A | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,064,710 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.891277 | 0.082143 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122102,"numValue":-0.891277388440431,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122103,"numValue":0.0821431640367561,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,634 | train | mutant | 476,753 | 358 | 286,819 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49M | F49M | 1 | 1 | 0 | 0 | 49 | F | M | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,407 | MegaScale | null | null | null | null | 4.481059 | null | null | null | null | null | null | 2.101979 | 1.111339 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367104,"numValue":2.101979368581969,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367105,"numValue":1.1113388638746584,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367106,"numValue":4.481059201100253,"references":[],"strValue":null,"typ... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,635 | train | mutant | 476,753 | 358 | 286,819 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49M | F49M | 1 | 1 | 0 | 0 | 49 | F | M | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,078 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.200249 | 0.054121 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122838,"numValue":-0.200249473853301,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122839,"numValue":0.054121394048165,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,637 | train | mutant | 476,754 | 358 | 286,820 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49L | F49L | 1 | 1 | 0 | 0 | 49 | F | L | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,077 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.061673 | 0.033884 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122836,"numValue":-0.0616729247757884,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122837,"numValue":0.0338837983249788,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,638 | train | mutant | 476,755 | 358 | 286,821 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49V | F49V | 1 | 1 | 0 | 0 | 49 | F | V | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,409 | MegaScale | null | null | null | null | 3.519179 | null | null | null | null | null | null | 1.506418 | 0.605379 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367110,"numValue":1.5064184927752056,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367111,"numValue":0.6053793774971137,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367112,"numValue":3.519178963939821,"references":[],"strValue":null,"ty... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,639 | train | mutant | 476,755 | 358 | 286,821 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49V | F49V | 1 | 1 | 0 | 0 | 49 | F | V | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,085 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.412384 | 0.036076 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122852,"numValue":-0.412384438018039,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122853,"numValue":0.0360756893145836,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,640 | train | mutant | 476,756 | 358 | 286,822 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49I | F49I | 1 | 1 | 0 | 0 | 49 | F | I | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,410 | MegaScale | null | null | null | null | 4.161329 | null | null | null | null | null | null | 1.979516 | 1.00304 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367113,"numValue":1.9795161671589137,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367114,"numValue":1.00304044449598,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367115,"numValue":4.161329336397861,"references":[],"strValue":null,"type... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,641 | train | mutant | 476,756 | 358 | 286,822 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49I | F49I | 1 | 1 | 0 | 0 | 49 | F | I | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,075 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.704137 | 0.114012 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122832,"numValue":-0.704136914862095,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122833,"numValue":0.114012261964352,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20644 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,644 | train | mutant | 476,758 | 358 | 286,824 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49Y | F49Y | 1 | 1 | 0 | 0 | 49 | F | Y | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,412 | MegaScale | null | null | null | null | 4.554099 | null | null | null | null | null | null | 2.032152 | 1.093478 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367119,"numValue":2.03215164051796,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367120,"numValue":1.0934779681461408,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367121,"numValue":4.554099471752039,"references":[],"strValue":null,"type... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,645 | train | mutant | 476,758 | 358 | 286,824 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49Y | F49Y | 1 | 1 | 0 | 0 | 49 | F | Y | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,087 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.276257 | 0.062367 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122856,"numValue":-0.276256994256532,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122857,"numValue":0.0623666846112341,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,646 | train | mutant | 476,759 | 358 | 286,825 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49P | F49P | 1 | 1 | 0 | 0 | 49 | F | P | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,413 | MegaScale | null | null | null | null | 0.07845 | null | null | null | null | null | null | -0.456864 | -1.762252 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367122,"numValue":-0.4568640893020833,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367123,"numValue":-1.7622517759383385,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367124,"numValue":0.0784502853396348,"references":[],"strValue":null,... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,647 | train | mutant | 476,759 | 358 | 286,825 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49P | F49P | 1 | 1 | 0 | 0 | 49 | F | P | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,080 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.859412 | 0.099809 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122842,"numValue":-0.859411970610982,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122843,"numValue":0.0998091071756823,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,648 | train | mutant | 476,760 | 358 | 286,826 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49C | F49C | 1 | 1 | 0 | 0 | 49 | F | C | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,414 | MegaScale | null | null | null | null | 3.760215 | null | null | null | null | null | null | 1.700752 | 0.65556 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367125,"numValue":1.7007523891561207,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367126,"numValue":0.6555598171720161,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367127,"numValue":3.760215422725926,"references":[],"strValue":null,"ty... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20649 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,649 | train | mutant | 476,760 | 358 | 286,826 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49C | F49C | 1 | 1 | 0 | 0 | 49 | F | C | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,064,711 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.320412 | 0.054424 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122104,"numValue":-0.320412038508792,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122105,"numValue":0.0544239165162376,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,651 | train | mutant | 476,762 | 358 | 478,095 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insA49 | insA49 | 1 | 0 | 0 | 1 | 49 | - | A | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,416 | MegaScale | null | null | null | null | 2.059616 | null | null | null | null | null | null | 0.436897 | -0.532091 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367131,"numValue":0.4368973018784804,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367132,"numValue":-0.532090709674861,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367133,"numValue":2.0596158052579256,"references":[],"strValue":null,"t... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,653 | train | mutant | 476,763 | 358 | 286,829 | 67 | 66 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | delF49 | delF49 | 1 | 0 | 1 | 0 | 49 | F | - | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,064,709 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.906691 | 0.091245 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122100,"numValue":-0.906690559499428,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122101,"numValue":0.0912449667757673,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,654 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,103 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E50K | 47.9 | null | null | null | null | null | 30.11 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|EASE-MM_S238.csv|HotMuSiC_S1626.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E50K","ty... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7857,"numValue":47.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","HotMuSiC_S1626.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,655 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,104 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E50K | 47.7 | null | null | null | null | null | 29.64 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|HotMuSiC_S1626.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E50K","ty... | [{"datasets":["EASE-MM_S238.csv","HotMuSiC_S1626.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7860,"numValue":47.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,656 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,148 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E50K | 49.7 | null | null | null | null | null | 31.55 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":7992,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7993,"numValue":31.55,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,657 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,149 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E50K | 49.7 | null | null | null | null | null | 31.31 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":7995,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7996,"numValue":31.31,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7997,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIB... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,658 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,194 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E50K | 50.7 | null | null | null | null | null | 32.5 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8130,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8131,"numValue":32.5,"references":[],"strValue":null,"type"... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,659 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,195 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E50K | 50.5 | null | null | null | null | null | 32.03 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8133,"numValue":50.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8134,"numValue":32.03,"references":[],"strValue":null,"type... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,660 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,240 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E50K | 52.2 | null | null | null | null | null | 33.7 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":8268,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8269,"numValue":33.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8270,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20661 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,661 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,241 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E50K | 52.3 | null | null | null | null | null | 33.46 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8271,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8272,"numValue":33.46,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8273,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,662 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,286 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E50K | 56.5 | null | null | null | null | null | 37.28 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8406,"numValue":56.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8407,"numValue":37.28,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","HotMuSiC_... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,663 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,287 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E50K | 55.7 | null | null | null | null | null | 36.33 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8409,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8410,"numValue":36.33,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S19... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,664 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,332 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E50K | 61 | null | null | null | null | null | 41.11 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8544,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8545,"numValue":41.11,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8546,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,665 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,333 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E50K | 60 | null | null | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8547,"numValue":60.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20666 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,666 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 7,262 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:E50K | null | null | 0.17 | 0.45 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25373,"numValue":0.17,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25374,"numValue":0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25375,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20667 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,667 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 7,263 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:E50K | null | null | 0.07 | 0.07 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25376,"numValue":0.07,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25377,"numValue":0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25378,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,668 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 7,296 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E50K | null | null | 0.69 | 0.41 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25475,"numValue":0.69,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25476,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25477,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,669 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 7,297 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E50K | null | null | 0.57 | -0.02 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25478,"numValue":0.57,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25479,"numValue":-0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25480,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,670 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,423 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.235974 | 1.499255 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367152,"numValue":2.2359738527404094,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367153,"numValue":1.4992549063864165,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367154,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,671 | train | mutant | 1,181 | 358 | 1,327 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50K | E50K | 1 | 1 | 0 | 0 | 50 | E | K | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,061 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.009995 | 0.060803 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122804,"numValue":-0.00999453321420433,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122805,"numValue":0.0608028759721669,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20672 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,672 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,105 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E50Q | 40.7 | null | null | null | null | null | 32.5 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E50Q","ty... | [{"datasets":["EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7863,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-M... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,673 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,150 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E50Q | 42.6 | null | null | null | null | null | 34.18 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7998,"numValue":42.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7999,"numValue":34.18,"references":[],"strValue":null,"type":"DHVH"},{"datase... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,674 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,196 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E50Q | 43.7 | null | null | null | null | null | 35.13 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8136,"numValue":43.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8137,"numValue":35.13,"references":[],"strValue":null,"type... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,675 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,242 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E50Q | 46.2 | null | null | null | null | null | 37.05 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8274,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8275,"numValue":37.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8276,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,677 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 2,334 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E50Q | 55.8 | null | null | null | null | null | 45.17 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,678 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 7,298 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E50Q | null | null | 0.12 | 0.96 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25481,"numValue":0.12,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25482,"numValue":0.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25483,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,680 | train | mutant | 1,182 | 358 | 1,328 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50Q | E50Q | 1 | 1 | 0 | 0 | 50 | E | Q | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,066 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.034437 | 0.060496 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122814,"numValue":0.034437131748679,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122815,"numValue":0.0604959189858287,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,681 | train | mutant | 476,764 | 358 | 478,096 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50N | E50N | 1 | 1 | 0 | 0 | 50 | E | N | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,419 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.440218 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367140,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367141,"numValue":1.4402179779821556,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367142,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,682 | train | mutant | 476,764 | 358 | 478,096 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50N | E50N | 1 | 1 | 0 | 0 | 50 | E | N | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,064 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.006882 | 0.111145 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122810,"numValue":-0.00688178353257886,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122811,"numValue":0.111145220168925,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,683 | train | mutant | 476,765 | 358 | 478,097 | 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 | E50H | E50H | 1 | 1 | 0 | 0 | 50 | E | H | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,420 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.533881 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367143,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367144,"numValue":1.5338814157423344,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367145,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,684 | train | mutant | 476,765 | 358 | 478,097 | 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 | E50H | E50H | 1 | 1 | 0 | 0 | 50 | E | H | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,059 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.010793 | 0.095012 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122800,"numValue":-0.0107925011621443,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122801,"numValue":0.0950120379077097,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,685 | train | mutant | 476,766 | 358 | 478,098 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50D | E50D | 1 | 1 | 0 | 0 | 50 | E | D | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,421 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.641812 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367146,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367147,"numValue":1.6418120356753922,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367148,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,686 | train | mutant | 476,766 | 358 | 478,098 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50D | E50D | 1 | 1 | 0 | 0 | 50 | E | D | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,064,717 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.035962 | 0.066291 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122116,"numValue":-0.0359619190804072,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122117,"numValue":0.066291141273877,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,687 | train | mutant | 476,767 | 358 | 478,099 | 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 | E50R | E50R | 1 | 1 | 0 | 0 | 50 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,422 | MegaScale | null | null | null | null | 4.781192 | null | null | null | null | null | null | null | 0.971029 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367149,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367150,"numValue":0.971029275851908,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367151,"numValue":4.781191683126352,"references":[],"strValue":null,"type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,688 | train | mutant | 476,767 | 358 | 478,099 | 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 | E50R | E50R | 1 | 1 | 0 | 0 | 50 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,067 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.022799 | 0.041076 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122816,"numValue":-0.0227988213626999,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122817,"numValue":0.0410755687913693,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,689 | train | mutant | 476,768 | 358 | 478,100 | 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 | E50T | E50T | 1 | 1 | 0 | 0 | 50 | E | T | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,424 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.686746 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367155,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367156,"numValue":1.686746427013544,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367157,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,690 | train | mutant | 476,768 | 358 | 478,100 | 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 | E50T | E50T | 1 | 1 | 0 | 0 | 50 | E | T | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,069 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.015808 | 0.048714 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122820,"numValue":0.0158078615851299,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122821,"numValue":0.0487135572914306,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,691 | train | mutant | 476,769 | 358 | 478,101 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50S | E50S | 1 | 1 | 0 | 0 | 50 | E | S | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,425 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.494094 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367158,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367159,"numValue":1.494093776553202,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367160,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,692 | train | mutant | 476,769 | 358 | 478,101 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50S | E50S | 1 | 1 | 0 | 0 | 50 | E | S | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,068 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.005199 | 0.042925 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122818,"numValue":0.00519936533027382,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122819,"numValue":0.0429251922529273,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,693 | train | mutant | 476,770 | 358 | 478,102 | 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 | E50A | E50A | 1 | 1 | 0 | 0 | 50 | E | A | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,426 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.630564 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367161,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367162,"numValue":1.6305639038944508,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367163,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,694 | train | mutant | 476,770 | 358 | 478,102 | 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 | E50A | E50A | 1 | 1 | 0 | 0 | 50 | E | A | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,064,715 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.052898 | 0.042112 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122112,"numValue":-0.0528977307472137,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122113,"numValue":0.0421122279050434,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,695 | train | mutant | 476,771 | 358 | 478,103 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50G | E50G | 1 | 1 | 0 | 0 | 50 | E | G | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,427 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.496314 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367164,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367165,"numValue":1.4963137481189666,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367166,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,696 | train | mutant | 476,771 | 358 | 478,103 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50G | E50G | 1 | 1 | 0 | 0 | 50 | E | G | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,058 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.115871 | 0.039932 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122798,"numValue":-0.115870956867839,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122799,"numValue":0.0399324199043506,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,697 | train | mutant | 476,772 | 358 | 478,104 | 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 | E50M | E50M | 1 | 1 | 0 | 0 | 50 | E | M | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,428 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.643188 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367167,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367168,"numValue":1.643188025587326,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367169,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,698 | train | mutant | 476,772 | 358 | 478,104 | 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 | E50M | E50M | 1 | 1 | 0 | 0 | 50 | E | M | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,063 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.03064 | 0.05552 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122808,"numValue":-0.0306404971616322,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122809,"numValue":0.0555195921371759,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,699 | train | mutant | 476,773 | 358 | 478,105 | 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 | E50L | E50L | 1 | 1 | 0 | 0 | 50 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,429 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.243993 | 1.547318 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367170,"numValue":2.243993115458601,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367171,"numValue":1.5473184822191102,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367172,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,700 | train | mutant | 476,773 | 358 | 478,105 | 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 | E50L | E50L | 1 | 1 | 0 | 0 | 50 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,062 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.114896 | 0.029648 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122806,"numValue":-0.114896344208902,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122807,"numValue":0.0296484531044787,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,701 | train | mutant | 476,774 | 358 | 478,106 | 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 | E50V | E50V | 1 | 1 | 0 | 0 | 50 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,430 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.477948 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367173,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367174,"numValue":1.4779478479066883,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367175,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,702 | train | mutant | 476,774 | 358 | 478,106 | 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 | E50V | E50V | 1 | 1 | 0 | 0 | 50 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,070 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.064637 | 0.040659 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122822,"numValue":-0.0646372438322015,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122823,"numValue":0.0406588958123121,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,703 | train | mutant | 476,775 | 358 | 478,107 | 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 | E50I | E50I | 1 | 1 | 0 | 0 | 50 | E | I | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,431 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.471171 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367176,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367177,"numValue":1.4711711198048496,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367178,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,704 | train | mutant | 476,775 | 358 | 478,107 | 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 | E50I | E50I | 1 | 1 | 0 | 0 | 50 | E | I | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,060 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.049756 | 0.062967 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122802,"numValue":-0.0497561536301131,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122803,"numValue":0.0629674606335301,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,705 | train | mutant | 476,776 | 358 | 478,108 | 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 | E50W | E50W | 1 | 1 | 0 | 0 | 50 | E | W | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,432 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.547945 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367179,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367180,"numValue":1.5479445274617385,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367181,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,706 | train | mutant | 476,776 | 358 | 478,108 | 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 | E50W | E50W | 1 | 1 | 0 | 0 | 50 | E | W | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,071 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.127487 | 0.038191 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122824,"numValue":-0.127486573315252,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122825,"numValue":0.0381906233184635,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,707 | train | mutant | 476,777 | 358 | 478,109 | 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 | E50Y | E50Y | 1 | 1 | 0 | 0 | 50 | E | Y | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,433 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.739377 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367182,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367183,"numValue":1.7393774973716682,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367184,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,708 | train | mutant | 476,777 | 358 | 478,109 | 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 | E50Y | E50Y | 1 | 1 | 0 | 0 | 50 | E | Y | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,072 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.098743 | 0.088717 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122826,"numValue":-0.0987431667477617,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122827,"numValue":0.0887173526993183,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,709 | train | mutant | 476,778 | 358 | 478,110 | 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 | E50F | E50F | 1 | 1 | 0 | 0 | 50 | E | F | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,434 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.699798 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367185,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367186,"numValue":1.6997978776209997,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367187,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,712 | train | mutant | 476,779 | 358 | 478,111 | 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 | E50P | E50P | 1 | 1 | 0 | 0 | 50 | E | P | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,065,065 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.102224 | 0.126112 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122812,"numValue":-1.10222396304495,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122813,"numValue":0.126111995322841,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,713 | train | mutant | 476,780 | 358 | 478,112 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50C | E50C | 1 | 1 | 0 | 0 | 50 | E | C | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,436 | MegaScale | null | null | null | null | 4.766511 | null | null | null | null | null | null | 2.002742 | 1.033343 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367191,"numValue":2.002742129329779,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367192,"numValue":1.033342618739863,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367193,"numValue":4.766511448750609,"references":[],"strValue":null,"type... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20714 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,714 | train | mutant | 476,780 | 358 | 478,112 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E50C | E50C | 1 | 1 | 0 | 0 | 50 | E | C | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,064,716 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.066588 | 0.065382 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122114,"numValue":-0.0665876958494565,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122115,"numValue":0.0653816663521205,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,715 | train | mutant | 476,781 | 358 | 478,113 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insG50 | insG50 | 1 | 0 | 0 | 1 | 50 | - | G | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,437 | MegaScale | null | null | null | null | 2.12106 | null | null | null | null | null | null | 0.467975 | -0.461261 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367194,"numValue":0.4679749332969295,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367195,"numValue":-0.4612611254340368,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367196,"numValue":2.121060161574057,"references":[],"strValue":null,"t... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,716 | train | mutant | 476,782 | 358 | 478,114 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insA50 | insA50 | 1 | 0 | 0 | 1 | 50 | - | A | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,438 | MegaScale | null | null | null | null | 2.665648 | null | null | null | null | null | null | 0.866762 | -0.092372 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367197,"numValue":0.8667623913882153,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367198,"numValue":-0.092371962518226,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367199,"numValue":2.6656480605112547,"references":[],"strValue":null,"t... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,717 | train | mutant | 476,783 | 358 | 478,115 | 67 | 66 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | delE50 | delE50 | 1 | 0 | 1 | 0 | 50 | E | - | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 502,439 | MegaScale | null | null | null | null | 2.55791 | null | null | null | null | null | null | 0.750122 | -0.367957 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367200,"numValue":0.7501221717049098,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367201,"numValue":-0.3679574241039424,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367202,"numValue":2.557909901804209,"references":[],"strValue":null,"t... | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,718 | train | mutant | 476,783 | 358 | 478,115 | 67 | 66 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | delE50 | delE50 | 1 | 0 | 1 | 0 | 50 | E | - | 4 | CONSERVATION | 1CSP | 247 | null | 50 | A | E | false | false | 67.91548 | 25.474444 | 5,064,714 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.11626 | 0.135521 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122110,"numValue":-1.11626009044577,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122111,"numValue":0.135520656912239,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20858,"numValue":4.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,719 | train | mutant | 476,784 | 358 | 478,116 | 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 | I51Q | I51Q | 1 | 1 | 0 | 0 | 51 | I | Q | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,440 | MegaScale | null | null | null | null | 4.632089 | null | null | null | null | null | null | 2.0822 | 1.216153 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367203,"numValue":2.082200284664732,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367204,"numValue":1.2161527769146558,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367205,"numValue":4.632089438134969,"references":[],"strValue":null,"typ... | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,720 | train | mutant | 476,784 | 358 | 478,116 | 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 | I51Q | I51Q | 1 | 1 | 0 | 0 | 51 | I | Q | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,065,050 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.097341 | 0.056239 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122782,"numValue":-0.0973410493542255,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122783,"numValue":0.0562389163877408,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,721 | train | mutant | 476,785 | 358 | 478,117 | 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 | I51E | I51E | 1 | 1 | 0 | 0 | 51 | I | E | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,441 | MegaScale | null | null | null | null | 3.613234 | null | null | null | null | null | null | 1.451981 | 0.788674 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367206,"numValue":1.451981049953623,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367207,"numValue":0.788674018048174,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367208,"numValue":3.613233972989316,"references":[],"strValue":null,"type... | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,722 | train | mutant | 476,785 | 358 | 478,117 | 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 | I51E | I51E | 1 | 1 | 0 | 0 | 51 | I | E | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,064,722 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.317683 | 0.043825 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122126,"numValue":-0.317682632384017,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122127,"numValue":0.0438251970554553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,723 | train | mutant | 476,786 | 358 | 478,118 | 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 | I51N | I51N | 1 | 1 | 0 | 0 | 51 | I | N | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,442 | MegaScale | null | null | null | null | 3.550023 | null | null | null | null | null | null | 1.451935 | 0.586068 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367209,"numValue":1.4519352192303874,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367210,"numValue":0.5860675828030427,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367211,"numValue":3.5500225409843917,"references":[],"strValue":null,"t... | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,724 | train | mutant | 476,786 | 358 | 478,118 | 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 | I51N | I51N | 1 | 1 | 0 | 0 | 51 | I | N | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,065,048 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.528282 | 0.059521 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122778,"numValue":-0.528282320937311,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122779,"numValue":0.0595213921958489,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,725 | train | mutant | 476,787 | 358 | 478,119 | 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 | I51H | I51H | 1 | 1 | 0 | 0 | 51 | I | H | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,443 | MegaScale | null | null | null | null | 4.227212 | null | null | null | null | null | null | 1.886963 | 0.920557 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367212,"numValue":1.886963495905712,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367213,"numValue":0.9205568135122304,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367214,"numValue":4.227212040394728,"references":[],"strValue":null,"typ... | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,726 | train | mutant | 476,787 | 358 | 478,119 | 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 | I51H | I51H | 1 | 1 | 0 | 0 | 51 | I | H | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,064,725 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.329831 | 0.059679 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122132,"numValue":-0.329830636363185,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122133,"numValue":0.059679078267898,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,727 | train | mutant | 476,788 | 358 | 478,120 | 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 | I51D | I51D | 1 | 1 | 0 | 0 | 51 | I | D | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,444 | MegaScale | null | null | null | null | 1.583213 | null | null | null | null | null | null | 0.189625 | -0.802064 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367215,"numValue":0.1896250888775179,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367216,"numValue":-0.8020642117221004,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367217,"numValue":1.5832127301199326,"references":[],"strValue":null,"... | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,728 | train | mutant | 476,788 | 358 | 478,120 | 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 | I51D | I51D | 1 | 1 | 0 | 0 | 51 | I | D | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,064,721 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.682841 | 0.088289 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122124,"numValue":-0.682841474926909,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122125,"numValue":0.0882889892751513,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,729 | train | mutant | 476,789 | 358 | 478,121 | 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 | I51R | I51R | 1 | 1 | 0 | 0 | 51 | I | R | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,445 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.216465 | 1.325957 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367218,"numValue":2.216464564578075,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367219,"numValue":1.3259574221835433,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367220,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,731 | train | mutant | 476,790 | 358 | 478,122 | 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 | I51K | I51K | 1 | 1 | 0 | 0 | 51 | I | K | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,446 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.130741 | 1.48463 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367221,"numValue":2.130741054228677,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367222,"numValue":1.4846302865861871,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367223,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,732 | train | mutant | 476,790 | 358 | 478,122 | 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 | I51K | I51K | 1 | 1 | 0 | 0 | 51 | I | K | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,065,045 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.008392 | 0.057498 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122772,"numValue":0.00839185047172427,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122773,"numValue":0.0574978166284376,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,733 | train | mutant | 476,791 | 358 | 478,123 | 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 | I51T | I51T | 1 | 1 | 0 | 0 | 51 | I | T | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 502,447 | MegaScale | null | null | null | null | 4.849738 | null | null | null | null | null | null | null | 1.361331 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367224,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367225,"numValue":1.36133104770111,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367226,"numValue":4.84973821533042,"references":[],"strValue":null,"type":"DG"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,734 | train | mutant | 476,791 | 358 | 478,123 | 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 | I51T | I51T | 1 | 1 | 0 | 0 | 51 | I | T | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,065,053 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.187193 | 0.043211 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122788,"numValue":-0.187193098981821,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122789,"numValue":0.0432108230705107,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,736 | train | mutant | 476,792 | 358 | 478,124 | 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 | I51S | I51S | 1 | 1 | 0 | 0 | 51 | I | S | 5 | CONSERVATION | 1CSP | 247 | null | 51 | A | E | false | false | 50.619433 | 21.08625 | 5,065,052 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.294213 | 0.036796 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12122786,"numValue":-0.294213419809097,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122787,"numValue":0.0367955655798703,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20859,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.