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:19955 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,955 | train | mutant | 476,506 | 358 | 477,858 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37M | G37M | 1 | 1 | 0 | 0 | 37 | G | M | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,142 | MegaScale | null | null | null | null | 4.949738 | null | null | null | null | null | null | null | 1.290323 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366309,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366310,"numValue":1.2903228118144006,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366311,"numValue":4.949737546159247,"references":[],"strValue":null,"type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19956 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,956 | train | mutant | 476,506 | 358 | 477,858 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37M | G37M | 1 | 1 | 0 | 0 | 37 | G | M | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,208 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.25424 | 0.061488 | 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":12123098,"numValue":-0.254240193749807,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123099,"numValue":0.0614882451838402,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19957 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,957 | train | mutant | 476,507 | 358 | 477,859 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37L | G37L | 1 | 1 | 0 | 0 | 37 | G | L | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,143 | MegaScale | null | null | null | null | 4.715302 | null | null | null | null | null | null | 2.18935 | 1.152118 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366312,"numValue":2.189349665493178,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366313,"numValue":1.152117958078848,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366314,"numValue":4.715302398814879,"references":[],"strValue":null,"type... | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19958 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,958 | train | mutant | 476,507 | 358 | 477,859 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37L | G37L | 1 | 1 | 0 | 0 | 37 | G | L | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,207 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.214632 | 0.045187 | 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":12123096,"numValue":-0.214631910756639,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123097,"numValue":0.0451866738984684,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19959 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,959 | train | mutant | 476,508 | 358 | 477,860 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37V | G37V | 1 | 1 | 0 | 0 | 37 | G | V | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,144 | MegaScale | null | null | null | null | 4.926475 | null | null | null | null | null | null | 2.089713 | 1.263946 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366315,"numValue":2.0897129645355883,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366316,"numValue":1.2639460638272273,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366317,"numValue":4.926474990499862,"references":[],"strValue":null,"ty... | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19960 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,960 | train | mutant | 476,508 | 358 | 477,860 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37V | G37V | 1 | 1 | 0 | 0 | 37 | G | V | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,215 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.230531 | 0.045247 | 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":12123112,"numValue":-0.230531161445722,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123113,"numValue":0.0452469477725991,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19961 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,961 | train | mutant | 476,509 | 358 | 477,861 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37I | G37I | 1 | 1 | 0 | 0 | 37 | G | I | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,145 | MegaScale | null | null | null | null | 4.604302 | null | null | null | null | null | null | 2.072403 | 1.089553 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366318,"numValue":2.072403246832879,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366319,"numValue":1.089552978210521,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366320,"numValue":4.604301525033534,"references":[],"strValue":null,"type... | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19962 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,962 | train | mutant | 476,509 | 358 | 477,861 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37I | G37I | 1 | 1 | 0 | 0 | 37 | G | I | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,205 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.275467 | 0.07185 | 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":12123092,"numValue":-0.275466999854575,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123093,"numValue":0.0718499295230538,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19963 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,963 | train | mutant | 476,510 | 358 | 477,862 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37W | G37W | 1 | 1 | 0 | 0 | 37 | G | W | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,146 | MegaScale | null | null | null | null | 4.931477 | null | null | null | null | null | null | 2.078628 | 1.293995 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366321,"numValue":2.0786275114193256,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366322,"numValue":1.2939950334585657,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366323,"numValue":4.931477291234884,"references":[],"strValue":null,"ty... | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19964 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,964 | train | mutant | 476,510 | 358 | 477,862 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37W | G37W | 1 | 1 | 0 | 0 | 37 | G | W | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,216 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.314907 | 0.053929 | 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":12123114,"numValue":-0.314906611682729,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123115,"numValue":0.0539287470437312,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19965 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,965 | train | mutant | 476,511 | 358 | 477,863 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37Y | G37Y | 1 | 1 | 0 | 0 | 37 | G | Y | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,147 | MegaScale | null | null | null | null | 4.873132 | null | null | null | null | null | null | null | 1.269359 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366324,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366325,"numValue":1.2693585588097145,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366326,"numValue":4.873131829544608,"references":[],"strValue":null,"type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,966 | train | mutant | 476,511 | 358 | 477,863 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37Y | G37Y | 1 | 1 | 0 | 0 | 37 | G | Y | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,217 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.236957 | 0.083902 | 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":12123116,"numValue":-0.236956612808226,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123117,"numValue":0.0839024962903077,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,967 | train | mutant | 476,512 | 358 | 477,864 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37F | G37F | 1 | 1 | 0 | 0 | 37 | G | F | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,148 | MegaScale | null | null | null | null | 4.685516 | null | null | null | null | null | null | 2.153877 | 1.156526 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366327,"numValue":2.1538774158701512,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366328,"numValue":1.1565256068614749,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366329,"numValue":4.685515786553015,"references":[],"strValue":null,"ty... | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19968 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,968 | train | mutant | 476,512 | 358 | 477,864 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37F | G37F | 1 | 1 | 0 | 0 | 37 | G | F | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,064,604 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.27263 | 0.063826 | 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":12121890,"numValue":-0.272630257533882,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121891,"numValue":0.0638257821910605,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19969 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,969 | train | mutant | 476,513 | 358 | 477,865 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37P | G37P | 1 | 1 | 0 | 0 | 37 | G | P | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,149 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.410083 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366330,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366331,"numValue":1.4100829486631223,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366332,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,970 | train | mutant | 476,513 | 358 | 477,865 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37P | G37P | 1 | 1 | 0 | 0 | 37 | G | P | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,065,210 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.145544 | 0.049413 | 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":12123102,"numValue":-0.145544201566826,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123103,"numValue":0.0494133831553198,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19971 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,971 | train | mutant | 476,514 | 358 | 477,866 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37C | G37C | 1 | 1 | 0 | 0 | 37 | G | C | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,150 | MegaScale | null | null | null | null | 4.710725 | null | null | null | null | null | null | 1.920275 | 1.09682 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366333,"numValue":1.9202745112573791,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366334,"numValue":1.096820399941159,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366335,"numValue":4.710725180134899,"references":[],"strValue":null,"typ... | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19972 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,972 | train | mutant | 476,514 | 358 | 477,866 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G37C | G37C | 1 | 1 | 0 | 0 | 37 | G | C | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,064,601 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.181947 | 0.063502 | 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":12121884,"numValue":-0.181947119075034,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121885,"numValue":0.0635024242339861,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,973 | train | mutant | 476,515 | 358 | 477,867 | 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 | insG37 | insG37 | 1 | 0 | 0 | 1 | 37 | - | G | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,151 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.955324 | 1.521694 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366336,"numValue":1.9553235922622,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366337,"numValue":1.5216940897136455,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366338,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19974 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,974 | train | mutant | 476,515 | 358 | 477,867 | 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 | insG37 | insG37 | 1 | 0 | 0 | 1 | 37 | - | G | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,173 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.826594 | 1.488268 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366402,"numValue":1.8265940421772024,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366403,"numValue":1.488267653593709,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366404,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,975 | train | mutant | 476,516 | 358 | 477,868 | 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 | insA37 | insA37 | 1 | 0 | 0 | 1 | 37 | - | A | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,152 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.97675 | 1.556069 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366339,"numValue":1.976750354045251,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366340,"numValue":1.556069181762906,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366341,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19976 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,976 | train | mutant | 476,517 | 358 | 477,869 | 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 | delG37 | delG37 | 1 | 0 | 1 | 0 | 37 | G | - | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 502,153 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.972866 | 1.520941 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366342,"numValue":1.9728655663051056,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366343,"numValue":1.5209409771736608,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366344,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19977 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,977 | train | mutant | 476,517 | 358 | 477,869 | 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 | delG37 | delG37 | 1 | 0 | 1 | 0 | 37 | G | - | 7 | CONSERVATION | 1CSP | 247 | null | 37 | A | S | true | false | 56.342682 | 36.445 | 5,064,599 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.167153 | 0.165013 | 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":12121880,"numValue":-1.16715330853397,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121881,"numValue":0.165013392797177,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20845,"numValue":7.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19978 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,978 | train | mutant | 1,769 | 358 | 1,982 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38A | F38A | 1 | 1 | 0 | 0 | 38 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 3,372 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | null | 1CSP_A:F38A | 62.1 | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:F38A",... | [{"datasets":[],"id":12430,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12431,"numValue":2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12432,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,979 | train | mutant | 1,769 | 358 | 1,982 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38A | F38A | 1 | 1 | 0 | 0 | 38 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 7,108 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | 60 | 1CSP_A:F38A | null | null | null | -0.31 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24937,"numValue":-0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24938,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19980 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,980 | train | mutant | 1,769 | 358 | 1,982 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38A | F38A | 1 | 1 | 0 | 0 | 38 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 10,702 | ProTherm | 7 | CD | Urea | Potassium phosphate | 0.35 M | 25 | 1CSP_A:F38A | null | null | 3.64 | -0.15 | null | null | null | 4.71 | 0.78 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"... | [{"datasets":[],"id":36747,"numValue":3.64,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36748,"numValue":-0.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36749,"numValue":0.78,"referen... | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19981 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,981 | train | mutant | 1,769 | 358 | 1,982 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38A | F38A | 1 | 1 | 0 | 0 | 38 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,163 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.419497 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366372,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366373,"numValue":1.4194971998281585,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366374,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19982 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,982 | train | mutant | 1,769 | 358 | 1,982 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38A | F38A | 1 | 1 | 0 | 0 | 38 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,064,606 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.025841 | 0.034269 | 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":12121894,"numValue":-0.0258410358298649,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121895,"numValue":0.0342685464526215,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19983 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,983 | train | mutant | 476,518 | 358 | 477,870 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38Q | F38Q | 1 | 1 | 0 | 0 | 38 | F | Q | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,154 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.218689 | 1.52778 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366345,"numValue":2.218689136040324,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366346,"numValue":1.5277804418262315,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366347,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19984 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,984 | train | mutant | 476,518 | 358 | 477,870 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38Q | F38Q | 1 | 1 | 0 | 0 | 38 | F | Q | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,197 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.056523 | 0.050143 | 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":12123076,"numValue":-0.0565226274207915,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123077,"numValue":0.0501433980909982,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19985 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,985 | train | mutant | 476,519 | 358 | 477,871 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38E | F38E | 1 | 1 | 0 | 0 | 38 | F | E | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,155 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.074038 | 1.492873 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366348,"numValue":2.074038152405789,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366349,"numValue":1.4928729125819966,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366350,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19986 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,986 | train | mutant | 476,519 | 358 | 477,871 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38E | F38E | 1 | 1 | 0 | 0 | 38 | F | E | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,064,609 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.004688 | 0.051245 | 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":12121900,"numValue":-0.00468844503770352,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121901,"numValue":0.0512446551941243,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19987 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,987 | train | mutant | 476,520 | 358 | 477,872 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38N | F38N | 1 | 1 | 0 | 0 | 38 | F | N | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,156 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.192115 | 1.517401 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366351,"numValue":2.1921152448763506,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366352,"numValue":1.5174010270477358,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366353,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19988 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,988 | train | mutant | 476,520 | 358 | 477,872 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38N | F38N | 1 | 1 | 0 | 0 | 38 | F | N | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,195 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.087094 | 0.108451 | 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":12123072,"numValue":-0.0870944294170362,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123073,"numValue":0.108451326991257,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19990 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,990 | train | mutant | 476,521 | 358 | 477,873 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38H | F38H | 1 | 1 | 0 | 0 | 38 | F | H | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,190 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.063821 | 0.063504 | 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":12123062,"numValue":-0.0638214887432237,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123063,"numValue":0.0635043869529971,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19991 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,991 | train | mutant | 476,522 | 358 | 477,874 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38D | F38D | 1 | 1 | 0 | 0 | 38 | F | D | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,158 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.557702 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366357,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366358,"numValue":1.5577023591240189,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366359,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19992 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,992 | train | mutant | 476,522 | 358 | 477,874 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38D | F38D | 1 | 1 | 0 | 0 | 38 | F | D | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,064,608 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.060187 | 0.073887 | 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":12121898,"numValue":-0.0601867784745906,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121899,"numValue":0.0738872318565488,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19993 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,993 | train | mutant | 476,523 | 358 | 477,875 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38R | F38R | 1 | 1 | 0 | 0 | 38 | F | R | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,159 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.648758 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366360,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366361,"numValue":1.6487575580658564,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366362,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19994 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,994 | train | mutant | 476,523 | 358 | 477,875 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38R | F38R | 1 | 1 | 0 | 0 | 38 | F | R | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,198 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.039169 | 0.029013 | 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":12123078,"numValue":-0.0391685112647498,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123079,"numValue":0.0290132804315136,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19995 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,995 | train | mutant | 476,524 | 358 | 477,876 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38K | F38K | 1 | 1 | 0 | 0 | 38 | F | K | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,160 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.193274 | 1.590661 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366363,"numValue":2.1932738218059797,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366364,"numValue":1.590661118561127,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366365,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19996 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,996 | train | mutant | 476,524 | 358 | 477,876 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38K | F38K | 1 | 1 | 0 | 0 | 38 | F | K | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,192 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.024725 | 0.054494 | 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":12123066,"numValue":-0.0247247393923163,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123067,"numValue":0.0544935869076338,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19997 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,997 | train | mutant | 476,525 | 358 | 477,877 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38T | F38T | 1 | 1 | 0 | 0 | 38 | F | T | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,161 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.134494 | 1.489867 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366366,"numValue":2.134493946770956,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366367,"numValue":1.4898674998553476,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366368,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19998 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,998 | train | mutant | 476,525 | 358 | 477,877 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38T | F38T | 1 | 1 | 0 | 0 | 38 | F | T | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,200 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.061827 | 0.05948 | 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":12123082,"numValue":-0.0618274888979105,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123083,"numValue":0.0594799788247153,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19999 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,999 | train | mutant | 476,526 | 358 | 477,878 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38S | F38S | 1 | 1 | 0 | 0 | 38 | F | S | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,162 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.532 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366369,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366370,"numValue":1.5320002015413356,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366371,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20000 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,000 | train | mutant | 476,526 | 358 | 477,878 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38S | F38S | 1 | 1 | 0 | 0 | 38 | F | S | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,199 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.08183 | 0.042076 | 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":12123080,"numValue":-0.0818300490195205,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123081,"numValue":0.042076156809718,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20001 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,001 | train | mutant | 476,527 | 358 | 477,879 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38G | F38G | 1 | 1 | 0 | 0 | 38 | F | G | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,164 | MegaScale | null | null | null | null | 4.990866 | null | null | null | null | null | null | 2.200647 | 1.436022 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366375,"numValue":2.200647175863561,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366376,"numValue":1.4360215484510004,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366377,"numValue":4.990866398230898,"references":[],"strValue":null,"typ... | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20002 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,002 | train | mutant | 476,527 | 358 | 477,879 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38G | F38G | 1 | 1 | 0 | 0 | 38 | F | G | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,189 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.094513 | 0.037285 | 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":12123060,"numValue":-0.0945128939292058,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123061,"numValue":0.0372849818322755,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20003 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,003 | train | mutant | 476,528 | 358 | 477,880 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38M | F38M | 1 | 1 | 0 | 0 | 38 | F | M | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,165 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.484459 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366378,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366379,"numValue":1.484459471040134,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366380,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20004 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,004 | train | mutant | 476,528 | 358 | 477,880 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38M | F38M | 1 | 1 | 0 | 0 | 38 | F | M | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,194 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.062795 | 0.042565 | 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":12123070,"numValue":-0.0627947413605556,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123071,"numValue":0.0425647757075249,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20005 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,005 | train | mutant | 476,529 | 358 | 477,881 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38L | F38L | 1 | 1 | 0 | 0 | 38 | F | L | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,166 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.529383 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366381,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366382,"numValue":1.529382538968636,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366383,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20006 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,006 | train | mutant | 476,529 | 358 | 477,881 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38L | F38L | 1 | 1 | 0 | 0 | 38 | F | L | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,193 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.067791 | 0.027346 | 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":12123068,"numValue":-0.0677910879431214,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123069,"numValue":0.0273460426340597,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20008 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,008 | train | mutant | 476,530 | 358 | 477,882 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38V | F38V | 1 | 1 | 0 | 0 | 38 | F | V | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,201 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.049305 | 0.03413 | 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":12123084,"numValue":-0.049305341607257,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123085,"numValue":0.0341298374200108,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20009 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,009 | train | mutant | 476,531 | 358 | 477,883 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38I | F38I | 1 | 1 | 0 | 0 | 38 | F | I | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,168 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.619978 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366387,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366388,"numValue":1.6199776502795735,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366389,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20010 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,010 | train | mutant | 476,531 | 358 | 477,883 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38I | F38I | 1 | 1 | 0 | 0 | 38 | F | I | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,191 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.114292 | 0.06534 | 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":12123064,"numValue":-0.114292194763306,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123065,"numValue":0.0653400812430734,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20012 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,012 | train | mutant | 476,532 | 358 | 477,884 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38W | F38W | 1 | 1 | 0 | 0 | 38 | F | W | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,202 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.027758 | 0.044364 | 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":12123086,"numValue":-0.027758366963808,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123087,"numValue":0.0443643682347913,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20013 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,013 | train | mutant | 476,533 | 358 | 477,885 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38Y | F38Y | 1 | 1 | 0 | 0 | 38 | F | Y | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,170 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.243273 | 1.741396 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366393,"numValue":2.243272658833569,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366394,"numValue":1.74139558385695,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366395,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20014 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,014 | train | mutant | 476,533 | 358 | 477,885 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38Y | F38Y | 1 | 1 | 0 | 0 | 38 | F | Y | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,203 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.088384 | 0.078969 | 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":12123088,"numValue":-0.0883836904674355,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123089,"numValue":0.0789686500412508,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20015 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,015 | train | mutant | 476,534 | 358 | 477,886 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38P | F38P | 1 | 1 | 0 | 0 | 38 | F | P | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,171 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.145891 | 1.667723 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366396,"numValue":2.1458910139056133,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366397,"numValue":1.6677233121049282,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366398,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20016 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,016 | train | mutant | 476,534 | 358 | 477,886 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38P | F38P | 1 | 1 | 0 | 0 | 38 | F | P | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,065,196 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.079417 | 0.044374 | 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":12123074,"numValue":-0.0794171313352812,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123075,"numValue":0.0443738751550011,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20017 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,017 | train | mutant | 476,535 | 358 | 477,887 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38C | F38C | 1 | 1 | 0 | 0 | 38 | F | C | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,172 | MegaScale | null | null | null | null | 4.850513 | null | null | null | null | null | null | 2.004114 | 1.256849 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366399,"numValue":2.004113527617048,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366400,"numValue":1.2568492363537316,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366401,"numValue":4.850513462771919,"references":[],"strValue":null,"typ... | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20018 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,018 | train | mutant | 476,535 | 358 | 477,887 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F38C | F38C | 1 | 1 | 0 | 0 | 38 | F | C | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,064,607 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.052627 | 0.058716 | 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":12121896,"numValue":-0.0526266301838091,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121897,"numValue":0.0587161621875681,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20019 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,019 | train | mutant | 476,536 | 358 | 477,888 | 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 | insA38 | insA38 | 1 | 0 | 0 | 1 | 38 | - | A | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,174 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.931768 | 1.512374 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366405,"numValue":1.9317684788617984,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366406,"numValue":1.5123740685921887,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366407,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20020 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,020 | train | mutant | 476,537 | 358 | 477,889 | 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 | delF38 | delF38 | 1 | 0 | 1 | 0 | 38 | F | - | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 502,175 | MegaScale | null | null | null | null | 4.997999 | null | null | null | null | null | null | 1.810506 | 1.375198 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366408,"numValue":1.8105059577001783,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366409,"numValue":1.375198462364726,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366410,"numValue":4.997998997181611,"references":[],"strValue":null,"typ... | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20021 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,021 | train | mutant | 476,537 | 358 | 477,889 | 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 | delF38 | delF38 | 1 | 0 | 1 | 0 | 38 | F | - | 5 | CONSERVATION | 1CSP | 247 | null | 38 | A | S | true | true | 163.731136 | 20.055454 | 5,064,605 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.115387 | 0.11051 | 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":12121892,"numValue":-1.11538743490596,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121893,"numValue":0.110510219233874,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20846,"numValue":5.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20022 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,022 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,064 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K39E | 50.7 | null | null | null | 34.18 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.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":"DSC","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:K39E","t... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7740,"numValue":50.7,"references":[],"strValue":null,"type":"T... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20023 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,023 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,094 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K39E | 51.4 | null | null | null | null | null | 34.66 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.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|_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:K39E","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.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"],... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20024 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,024 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,139 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:K39E | 52.8 | null | null | null | null | null | 35.85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|STRUM_Q3421.csv|EASE-MM_S238.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"],"id":7965,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","M47andM8_S2760.csv","STRUM_Q3421.csv"],"id":7966,"numValue":35.85,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["EASE-MM_S238.csv","M47andM8_S2760.c... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20025 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,025 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,185 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:K39E | 53.7 | null | null | null | null | null | 36.57 | 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":8103,"numValue":53.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8104,"numValue":36.57,"references":[],"strValue":null,"type... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20026 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,026 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,231 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:K39E | 55.2 | null | null | null | null | null | 37.76 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|HotMuSiC_S1626.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","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8241,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets"... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20027 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,027 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,277 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K39E | 58.9 | null | null | null | null | null | 40.87 | 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"],"id":8379,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8380,"numValue":40.87,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20028 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,028 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,323 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K39E | 63.6 | null | null | null | null | null | 44.93 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.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_S2204.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|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":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.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_S2204.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8517,"numValue":6... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20029 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,029 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,226 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:K39E | null | null | 0.02 | 0.31 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.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":25265,"numValue":0.02,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25266,"numValue":0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25267,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20030 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,030 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,253 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:K39E | null | null | 0.45 | 0.17 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.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":25346,"numValue":0.45,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25347,"numValue":0.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25348,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20031 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,031 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,287 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:K39E | null | null | 1.05 | 0.05 | 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":25448,"numValue":1.05,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25449,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25450,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20032 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,032 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,177 | MegaScale | null | null | null | null | 4.433931 | null | null | null | null | null | null | 2.003367 | 1.099196 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366414,"numValue":2.00336722079254,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366415,"numValue":1.0991956567187169,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366416,"numValue":4.43393106575758,"references":[],"strValue":null,"type"... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20033 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,033 | train | mutant | 1,155 | 358 | 1,301 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39E | K39E | 1 | 1 | 0 | 0 | 39 | K | E | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,614 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.19192 | 0.053698 | 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":12121910,"numValue":-0.191920185050055,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121911,"numValue":0.0536979987564948,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20034 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,034 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,095 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:K39Q | 53.4 | null | null | null | null | null | 34.18 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.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:K39Q","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7833,"numValue":53.4,"referenc... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20035 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,035 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,140 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:K39Q | 54.9 | null | null | null | null | null | 35.37 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|khan_protherm_data_mapped.csv|M47andM8_S2760.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":["EASE-MM_S238.csv","khan_protherm_data_mapped.csv","M47andM8_S2760.csv"],"id":7968,"numValue":54.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":7969,"numValue":35.37,"references":[],"strValue":null,"type":"DHVH"},... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20036 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,036 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,186 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:K39Q | 55.7 | null | null | null | null | null | 36.09 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S238.csv|khan_protherm_data_mapped.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","khan_protherm_data_mapped.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8106,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","khan_protherm_data_mapped.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20037 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,037 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,232 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:K39Q | 56.8 | null | null | null | null | null | 37.05 | 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|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|Broom_S605.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","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":824... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20038 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,038 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,278 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K39Q | 59.9 | null | null | null | null | null | 39.67 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|khan_protherm_data_mapped.csv|Saraboji_S2204.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","khan_protherm_data_mapped.csv","Saraboji_S2204.csv"],"id":8382,"numValue":59.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","khan_protherm_data_mapped.csv","Saraboji_S2204.csv"],"id":8383,"numValue":39.67,"references":[],"strValue":null,"type":"DHVH"... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20039 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,039 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 2,324 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K39Q | 64.4 | null | null | null | null | null | 43.5 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S2204.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3... | 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","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S2204.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20040 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,040 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,194 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:K39Q | null | null | 0 | 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":["khan_protherm_data_mapped.csv"],"id":25169,"numValue":0.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25170,"numValue":0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25171,"numValue":null,"reference... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20041 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,041 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,208 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:K39Q | null | null | 0.07 | 0.1 | 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":["khan_protherm_data_mapped.csv"],"id":25211,"numValue":0.07,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25212,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25213,"numValue":null,"reference... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20042 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,042 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,227 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:K39Q | null | null | 0.19 | 0.14 | 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":["khan_protherm_data_mapped.csv"],"id":25268,"numValue":0.19,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25269,"numValue":0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25270,"numValue":null,"referenc... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20044 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,044 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 7,288 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:K39Q | null | null | 1.1 | 0 | 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":["khan_protherm_data_mapped.csv"],"id":25451,"numValue":1.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25452,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25453,"numValue":null,"references... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20045 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,045 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,176 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366411,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366412,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366413,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20046 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,046 | train | mutant | 1,176 | 358 | 1,322 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39Q | K39Q | 1 | 1 | 0 | 0 | 39 | K | Q | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,182 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.109347 | 0.047727 | 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":12123046,"numValue":-0.109347369554781,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123047,"numValue":0.047726665371681,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20047 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,047 | train | mutant | 476,538 | 358 | 477,890 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39N | K39N | 1 | 1 | 0 | 0 | 39 | K | N | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,178 | MegaScale | null | null | null | null | 4.897547 | null | null | null | null | null | null | 2.127777 | 1.352924 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366417,"numValue":2.127777108507116,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366418,"numValue":1.3529240706910093,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366419,"numValue":4.897546703547069,"references":[],"strValue":null,"typ... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20048 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,048 | train | mutant | 476,538 | 358 | 477,890 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39N | K39N | 1 | 1 | 0 | 0 | 39 | K | N | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,180 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.143241 | 0.071983 | 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":12123042,"numValue":-0.143241073477269,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123043,"numValue":0.0719833330808377,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20049 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,049 | train | mutant | 476,539 | 358 | 477,891 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39H | K39H | 1 | 1 | 0 | 0 | 39 | K | H | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,179 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.192892 | 1.418353 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366420,"numValue":2.1928915453029134,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366421,"numValue":1.4183528286874925,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366422,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20050 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,050 | train | mutant | 476,539 | 358 | 477,891 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39H | K39H | 1 | 1 | 0 | 0 | 39 | K | H | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,617 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.21191 | 0.098919 | 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":12121916,"numValue":-0.211910478177846,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121917,"numValue":0.0989192594440366,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20051 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,051 | train | mutant | 476,540 | 358 | 477,892 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39D | K39D | 1 | 1 | 0 | 0 | 39 | K | D | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,180 | MegaScale | null | null | null | null | 4.413028 | null | null | null | null | null | null | 2.034523 | 1.056465 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366423,"numValue":2.034522857065396,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366424,"numValue":1.0564650271010778,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366425,"numValue":4.413027805828143,"references":[],"strValue":null,"typ... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20052 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,052 | train | mutant | 476,540 | 358 | 477,892 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39D | K39D | 1 | 1 | 0 | 0 | 39 | K | D | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,064,613 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.137584 | 0.068057 | 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":12121908,"numValue":-0.137584149277538,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121909,"numValue":0.0680569136991838,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20054 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,054 | train | mutant | 476,541 | 358 | 477,893 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39R | K39R | 1 | 1 | 0 | 0 | 39 | K | R | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,183 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.045346 | 0.039055 | 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":12123048,"numValue":-0.0453455560024148,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123049,"numValue":0.0390551949093448,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20055 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,055 | train | mutant | 476,542 | 358 | 477,894 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39T | K39T | 1 | 1 | 0 | 0 | 39 | K | T | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,182 | MegaScale | null | null | null | null | 4.843419 | null | null | null | null | null | null | 2.082191 | 1.307894 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366429,"numValue":2.0821913217520227,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366430,"numValue":1.3078937209688677,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366431,"numValue":4.8434187870943575,"references":[],"strValue":null,"t... | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20056 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,056 | train | mutant | 476,542 | 358 | 477,894 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39T | K39T | 1 | 1 | 0 | 0 | 39 | K | T | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,185 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.165129 | 0.042947 | 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":12123052,"numValue":-0.165129070548892,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123053,"numValue":0.0429467698950553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20057 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,057 | train | mutant | 476,543 | 358 | 477,895 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39S | K39S | 1 | 1 | 0 | 0 | 39 | K | S | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,183 | MegaScale | null | null | null | null | 4.917558 | null | null | null | null | null | null | null | 1.351395 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366432,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366433,"numValue":1.351395001798844,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366434,"numValue":4.917557805694395,"references":[],"strValue":null,"type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20058 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,058 | train | mutant | 476,543 | 358 | 477,895 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39S | K39S | 1 | 1 | 0 | 0 | 39 | K | S | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 5,065,184 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.111652 | 0.036614 | 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":12123050,"numValue":-0.11165172434372,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123051,"numValue":0.0366143698141667,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20059 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,059 | train | mutant | 476,544 | 358 | 477,896 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K39A | K39A | 1 | 1 | 0 | 0 | 39 | K | A | 4 | CONSERVATION | 1CSP | 247 | null | 39 | A | L | true | true | 73.576477 | 27.417778 | 502,184 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.153158 | 1.457908 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366435,"numValue":2.1531576418509264,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366436,"numValue":1.4579078751145709,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366437,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20847,"numValue":4.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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