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:20514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,514 | train | mutant | 476,716 | 358 | 478,068 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47W | V47W | 1 | 1 | 0 | 0 | 47 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,366 | MegaScale | null | null | null | null | 1.17162 | null | null | null | null | null | null | -0.021065 | -1.648944 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366981,"numValue":-0.021064653789219,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366982,"numValue":-1.6489439340340362,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366983,"numValue":1.1716198750363174,"references":[],"strValue":null,"... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,515 | train | mutant | 476,716 | 358 | 478,068 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47W | V47W | 1 | 1 | 0 | 0 | 47 | V | W | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,065,092 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.123781 | 0.105193 | 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":12122866,"numValue":-1.12378110702627,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122867,"numValue":0.105193090762935,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,516 | train | mutant | 476,717 | 358 | 478,069 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47Y | V47Y | 1 | 1 | 0 | 0 | 47 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,367 | MegaScale | null | null | null | null | 3.005906 | null | null | null | null | null | null | 1.117016 | -0.122058 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366984,"numValue":1.117016032007384,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366985,"numValue":-0.1220576811090937,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366986,"numValue":3.0059057308716004,"references":[],"strValue":null,"t... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,517 | train | mutant | 476,717 | 358 | 478,069 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47Y | V47Y | 1 | 1 | 0 | 0 | 47 | V | Y | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,065,093 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.995475 | 0.134173 | 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":12122868,"numValue":-0.995474951319969,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122869,"numValue":0.134173495651013,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,519 | train | mutant | 476,718 | 358 | 478,070 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47F | V47F | 1 | 1 | 0 | 0 | 47 | V | F | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,680 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.044861 | 0.128277 | 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":12122042,"numValue":-1.04486053746729,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122043,"numValue":0.12827656771721,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,520 | train | mutant | 476,719 | 358 | 478,071 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47P | V47P | 1 | 1 | 0 | 0 | 47 | V | P | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,369 | MegaScale | null | null | null | null | 0.501578 | null | null | null | null | null | null | -0.566314 | -1.513255 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366990,"numValue":-0.5663140973964753,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366991,"numValue":-1.5132550809534018,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366992,"numValue":0.5015777822143204,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,522 | train | mutant | 476,720 | 358 | 478,072 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47C | V47C | 1 | 1 | 0 | 0 | 47 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,370 | MegaScale | null | null | null | null | 4.403114 | null | null | null | null | null | null | 1.87785 | 0.953852 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366993,"numValue":1.8778497393553848,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366994,"numValue":0.9538516920709236,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366995,"numValue":4.403113695273151,"references":[],"strValue":null,"ty... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,523 | train | mutant | 476,720 | 358 | 478,072 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V47C | V47C | 1 | 1 | 0 | 0 | 47 | V | C | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,677 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.102671 | 0.074236 | 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":12122036,"numValue":-0.102671058168674,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122037,"numValue":0.0742357984859218,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,524 | train | mutant | 476,721 | 358 | 478,073 | 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 | insG47 | insG47 | 1 | 0 | 0 | 1 | 47 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,371 | MegaScale | null | null | null | null | 1.58483 | null | null | null | null | null | null | 0.052591 | -0.809066 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2366996,"numValue":0.0525909938708725,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366997,"numValue":-0.8090660652788223,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366998,"numValue":1.5848298898367492,"references":[],"strValue":null,"... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,525 | train | mutant | 476,722 | 358 | 478,074 | 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 | delV47 | delV47 | 1 | 0 | 1 | 0 | 47 | V | - | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 502,373 | MegaScale | null | null | null | null | 0.347572 | null | null | null | null | null | null | -0.64482 | -1.606569 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367002,"numValue":-0.6448200532196064,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367003,"numValue":-1.6065693321206334,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367004,"numValue":0.3475719004740095,"references":[],"strValue":null,... | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,526 | train | mutant | 476,722 | 358 | 478,074 | 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 | delV47 | delV47 | 1 | 0 | 1 | 0 | 47 | V | - | 9 | CONSERVATION | 1CSP | 247 | null | 47 | A | E | false | false | 1.13102 | 27.545715 | 5,064,675 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.114809 | 0.098059 | 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":12122032,"numValue":-1.11480853706714,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122033,"numValue":0.0980586684926496,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20855,"numValue":9.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,527 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 1,762 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:S48R | 62.7 | 8.9 | null | null | null | null | 48.28 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":["EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6592,"numValue":... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,528 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,342 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:S48R | 62.7 | 8.9 | null | -1.58 | 48.48 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19509,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19510,"numValue":8.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19511,"numValue":48.48,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv","potapov_wit... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:20529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,529 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,359 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:S48R | 62.7 | 8.9 | null | -0.62 | 48.48 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19611,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19612,"numValue":8.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19613,"numValue":48.48,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19614,"numValue":-0.62,"references":[... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,530 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,376 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:S48R | 62.7 | 7.7 | null | -0.96 | 48.48 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19713,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19714,"numValue":7.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19715,"numValue":48.48,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19716,"numValue":-0.96,"references":[... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,531 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,386 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:S48R | 62.7 | 8.9 | null | -0.96 | 48.48 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19773,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19774,"numValue":8.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19775,"numValue":48.48,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19776,"numValue":-0.96,"references":[... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,532 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 6,678 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:S48R | null | null | null | -1.58 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23789,"numValue":-1.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23790,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,533 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,379 | 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":2367020,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367021,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367022,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,534 | train | mutant | 988 | 358 | 1,115 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48R | S48R | 1 | 1 | 0 | 0 | 48 | S | R | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,708 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.024401 | 0.040709 | 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":12122098,"numValue":0.0244008907554893,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122099,"numValue":0.0407089022126161,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,535 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,066 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:S48E | 49.3 | 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|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.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":"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:S48E","t... | [{"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","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7746,"numVal... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,536 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,102 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:S48E | 51 | null | null | null | null | null | 36.33 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.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:S48E","ty... | [{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7854,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7855,"n... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,537 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,147 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:S48E | 53 | null | null | null | null | null | 38 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":["khan_protherm_data_mapped.csv"],"id":7989,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":7990,"numValue":38.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":7991,"numValue":null,"references... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,538 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,193 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:S48E | 54 | null | null | null | null | null | 38.96 | 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":8127,"numValue":54.0,"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":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,539 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,239 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:S48E | 55.6 | null | null | null | null | null | 40.15 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":["khan_protherm_data_mapped.csv"],"id":8265,"numValue":55.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":8266,"numValue":40.15,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.csv","STRUM_Q3421.csv"],"id":8267,"numValu... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,540 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,285 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:S48E | 58.9 | null | null | null | null | null | 43.02 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|khan_protherm_data_mapped.csv|Saraboji_S2204.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.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_S1962.csv","khan_protherm_data_mapped.csv","Saraboji_S2204.csv"],"id":8403,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","khan_protherm_data_mapped.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":8404,"numValue":43.02,"r... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20541 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,541 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,331 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:S48E | 63.5 | null | null | null | null | null | 46.85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|khan_protherm_data_mapped.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_S1676.csv","khan_protherm_data_mapped.csv"],"id":8541,"numValue":63.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","khan_protherm_data_mapped.csv"],"id":8542,"numValue":46.85,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.cs... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,542 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,234 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:S48E | null | null | 0.07 | -0.05 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|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":["khan_protherm_data_mapped.csv"],"id":25289,"numValue":0.07,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25290,"numValue":-0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,543 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,261 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:S48E | null | null | 0.48 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|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":["khan_protherm_data_mapped.csv"],"id":25370,"numValue":0.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25371,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"i... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,544 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,295 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:S48E | null | null | 1.1 | -0.02 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|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":["khan_protherm_data_mapped.csv"],"id":25472,"numValue":1.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25473,"numValue":-0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,546 | train | mutant | 1,157 | 358 | 1,303 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48E | S48E | 1 | 1 | 0 | 0 | 48 | S | E | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,697 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.036496 | 0.055687 | 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":12122076,"numValue":-0.036495533311543,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122077,"numValue":0.0556870366028082,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,547 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,100 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:S48K | 60.5 | null | null | null | null | null | 40.63 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.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 | 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:S48K","ty... | [{"datasets":["AUTOMUTE_S1925.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":7848,"numValue":60.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:20549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,549 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,145 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:S48K | 61.6 | null | null | null | null | null | 41.59 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":7983,"numValue":61.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7984,"numValue":41.59,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":7985,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,550 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,146 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:S48K | 56.8 | null | null | null | null | null | 38.48 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":7986,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7987,"numValue":38.48,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":7988,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,551 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,191 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:S48K | 62.2 | null | null | null | null | null | 42.07 | 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":8121,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8122,"numValue":42.07,"references":[],"strValue":null,"type... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,552 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,192 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:S48K | 57.4 | null | null | null | null | null | 38.96 | 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":8124,"numValue":57.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8125,"numValue":38.96,"references":[],"strValue":null,"type... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,553 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,237 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:S48K | 62.9 | null | null | null | null | null | 42.54 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8259,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8260,"numValue":42.54,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8261,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,554 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,238 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:S48K | 58.6 | null | null | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | STRUM_Q3421.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.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":["STRUM_Q3421.csv"],"id":8262,"numValue":58.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv"],"id":8263,"numValue":39.91,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8264,"numValue":null,"references":[],"strValue":"Unknown","type"... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,555 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,283 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:S48K | 64.8 | null | null | null | null | null | 44.22 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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":[],"id":8397,"numValue":64.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8398,"numValue":44.22,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["Broom_S605.csv"],"id":8399,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,556 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,284 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:S48K | 61.4 | null | null | null | null | null | 42.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8400,"numValue":61.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8401,"numValue":42.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8402,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,557 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,329 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:S48K | 68 | null | null | null | null | null | 46.85 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8535,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8536,"numValue":46.85,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8537,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,558 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 2,330 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:S48K | 65.3 | null | null | null | null | null | 45.41 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.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_S1676.csv"],"id":8538,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv"],"id":8539,"numValue":45.41,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["EASE-MM_S1676.csv"],"id":8540,"numValue":null,"references":[],"strValue":"Unknown","type":"R... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,559 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,341 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:S48K | 61.5 | 7.7 | null | -1.42 | 46.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19503,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19504,"numValue":7.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19505,"numValue":46.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19506,"numValue":-1.42,"references":[]... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,560 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,358 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:S48K | 61.5 | 7.7 | null | -0.74 | 46.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19605,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19606,"numValue":7.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19607,"numValue":46.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19608,"numValue":-0.74,"references":[]... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,561 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,375 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:S48K | 61.5 | 23.2 | null | -0.62 | 46.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":19707,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19708,"numValue":23.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19709,"numValue":46.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19710,"numValue":-0.62,"references":[... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,563 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,186 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:S48K | null | null | 0.05 | -0.76 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|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":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":25145,"numValue":0.05,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25146,"numValue":-0.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25147,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:20564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,564 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,198 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:S48K | null | null | 0.76 | -0.74 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25181,"numValue":0.76,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25182,"numValue":-0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25183,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,565 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,199 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:S48K | null | null | 0.22 | -0.81 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25184,"numValue":0.22,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25185,"numValue":-0.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25186,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,566 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,212 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:S48K | null | null | 0.84 | -0.67 | 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":25223,"numValue":0.84,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25224,"numValue":-0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25225,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,567 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,213 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:S48K | null | null | 0.29 | -0.79 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25226,"numValue":0.29,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25227,"numValue":-0.79,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25228,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,568 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,232 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:S48K | null | null | 0.93 | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25283,"numValue":0.93,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25284,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25285,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,569 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,233 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:S48K | null | null | 0.41 | -0.65 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25286,"numValue":0.41,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25287,"numValue":-0.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25288,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,570 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,259 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:S48K | null | null | 1.17 | -0.55 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25364,"numValue":1.17,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25365,"numValue":-0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25366,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,572 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,293 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:S48K | null | null | 1.58 | -0.48 | 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":25466,"numValue":1.58,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25467,"numValue":-0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25468,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:20573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,573 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 7,294 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:S48K | null | null | 1.24 | -0.69 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25469,"numValue":1.24,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25470,"numValue":-0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25471,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:20574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,574 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,380 | 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":2367023,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367024,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367025,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,575 | train | mutant | 1,180 | 358 | 1,326 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48K | S48K | 1 | 1 | 0 | 0 | 48 | S | K | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,702 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.015521 | 0.060815 | 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":12122086,"numValue":0.0155214272794514,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122087,"numValue":0.0608146952207117,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,576 | train | mutant | 476,723 | 358 | 478,075 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48Q | S48Q | 1 | 1 | 0 | 0 | 48 | S | Q | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,374 | 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":2367005,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367006,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367007,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,577 | train | mutant | 476,723 | 358 | 478,075 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48Q | S48Q | 1 | 1 | 0 | 0 | 48 | S | Q | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,707 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.004358 | 0.058134 | 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":12122096,"numValue":0.00435846290396671,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122097,"numValue":0.0581338234569824,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,578 | train | mutant | 476,724 | 358 | 478,076 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48N | S48N | 1 | 1 | 0 | 0 | 48 | S | N | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,376 | 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":2367011,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367012,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367013,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,579 | train | mutant | 476,724 | 358 | 478,076 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48N | S48N | 1 | 1 | 0 | 0 | 48 | S | N | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,705 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.03163 | 0.0824 | 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":12122092,"numValue":-0.0316304435628428,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122093,"numValue":0.0824002188922377,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,580 | train | mutant | 476,725 | 358 | 478,077 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48H | S48H | 1 | 1 | 0 | 0 | 48 | S | H | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,377 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.208848 | 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":2367014,"numValue":2.2088480608547254,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367015,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367016,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,581 | train | mutant | 476,725 | 358 | 478,077 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48H | S48H | 1 | 1 | 0 | 0 | 48 | S | H | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,700 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.048594 | 0.07073 | 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":12122082,"numValue":-0.0485938559657426,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122083,"numValue":0.0707297689824523,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,582 | train | mutant | 476,726 | 358 | 478,078 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48D | S48D | 1 | 1 | 0 | 0 | 48 | S | D | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,378 | MegaScale | null | null | null | null | 4.396127 | null | null | null | null | null | null | null | 0.994983 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367017,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367018,"numValue":0.994982896536885,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367019,"numValue":4.396126624301048,"references":[],"strValue":null,"type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,583 | train | mutant | 476,726 | 358 | 478,078 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48D | S48D | 1 | 1 | 0 | 0 | 48 | S | D | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,696 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.141792 | 0.061853 | 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":12122074,"numValue":-0.14179234150722,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122075,"numValue":0.0618525749002709,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,584 | train | mutant | 476,727 | 358 | 478,079 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48T | S48T | 1 | 1 | 0 | 0 | 48 | S | T | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,381 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.204577 | 1.677416 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367026,"numValue":2.204576897821936,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367027,"numValue":1.6774155934592412,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367028,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,585 | train | mutant | 476,727 | 358 | 478,079 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48T | S48T | 1 | 1 | 0 | 0 | 48 | S | T | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,065,088 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.019648 | 0.052119 | 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":12122858,"numValue":0.0196480440002349,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122859,"numValue":0.0521190587805516,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,586 | train | mutant | 476,728 | 358 | 478,080 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48A | S48A | 1 | 1 | 0 | 0 | 48 | S | A | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,382 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.24048 | 1.723286 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367029,"numValue":2.240480055543678,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367030,"numValue":1.7232855916430745,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367031,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,587 | train | mutant | 476,728 | 358 | 478,080 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48A | S48A | 1 | 1 | 0 | 0 | 48 | S | A | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,694 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.016916 | 0.049104 | 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":12122070,"numValue":-0.0169161844766958,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122071,"numValue":0.0491043346465355,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,588 | train | mutant | 476,729 | 358 | 478,081 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48G | S48G | 1 | 1 | 0 | 0 | 48 | S | G | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,383 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.469169 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367032,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367033,"numValue":1.469169062872878,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367034,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,589 | train | mutant | 476,729 | 358 | 478,081 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48G | S48G | 1 | 1 | 0 | 0 | 48 | S | G | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,699 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.116338 | 0.038232 | 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":12122080,"numValue":-0.116338329332351,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122081,"numValue":0.038232453767387,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,590 | train | mutant | 476,730 | 358 | 478,082 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48M | S48M | 1 | 1 | 0 | 0 | 48 | S | M | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,384 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.231006 | 1.646948 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367035,"numValue":2.231006167239451,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367036,"numValue":1.646948403405455,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367037,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,591 | train | mutant | 476,730 | 358 | 478,082 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48M | S48M | 1 | 1 | 0 | 0 | 48 | S | M | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,704 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.03011 | 0.062113 | 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":12122090,"numValue":0.0301099496789513,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122091,"numValue":0.062113125848991,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,592 | train | mutant | 476,731 | 358 | 478,083 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48L | S48L | 1 | 1 | 0 | 0 | 48 | S | L | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,385 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.077657 | 1.703833 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367038,"numValue":2.0776569201929984,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367039,"numValue":1.7038331368378787,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367040,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,593 | train | mutant | 476,731 | 358 | 478,083 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48L | S48L | 1 | 1 | 0 | 0 | 48 | S | L | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,703 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.037056 | 0.038824 | 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":12122088,"numValue":-0.03705552157939,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122089,"numValue":0.0388237106024793,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,594 | train | mutant | 476,732 | 358 | 478,084 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48V | S48V | 1 | 1 | 0 | 0 | 48 | S | V | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,386 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.74429 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367041,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367042,"numValue":1.744290121349481,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367043,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,595 | train | mutant | 476,732 | 358 | 478,084 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48V | S48V | 1 | 1 | 0 | 0 | 48 | S | V | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,065,089 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.050853 | 0.047722 | 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":12122860,"numValue":-0.0508534362272419,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122861,"numValue":0.0477222492539061,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,597 | train | mutant | 476,733 | 358 | 478,085 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48I | S48I | 1 | 1 | 0 | 0 | 48 | S | I | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,701 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.008153 | 0.068142 | 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":12122084,"numValue":-0.00815264409224953,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122085,"numValue":0.0681418012964127,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,598 | train | mutant | 476,734 | 358 | 478,086 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48W | S48W | 1 | 1 | 0 | 0 | 48 | S | W | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,388 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.13693 | 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":2367047,"numValue":2.136929681810716,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367048,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367049,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,599 | train | mutant | 476,734 | 358 | 478,086 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48W | S48W | 1 | 1 | 0 | 0 | 48 | S | W | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,065,090 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.019457 | 0.048414 | 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":12122862,"numValue":0.0194566788966551,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122863,"numValue":0.0484135127561095,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,600 | train | mutant | 476,735 | 358 | 478,087 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48Y | S48Y | 1 | 1 | 0 | 0 | 48 | S | Y | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,389 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.619204 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367050,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367051,"numValue":1.6192035650578602,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367052,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,601 | train | mutant | 476,735 | 358 | 478,087 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48Y | S48Y | 1 | 1 | 0 | 0 | 48 | S | Y | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,065,091 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.042855 | 0.052777 | 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":12122864,"numValue":-0.0428547429074235,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122865,"numValue":0.0527765267147831,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,602 | train | mutant | 476,736 | 358 | 478,088 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48F | S48F | 1 | 1 | 0 | 0 | 48 | S | F | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,390 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.745083 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367053,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2367054,"numValue":1.7450826209467911,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367055,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,603 | train | mutant | 476,736 | 358 | 478,088 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48F | S48F | 1 | 1 | 0 | 0 | 48 | S | F | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,698 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.017851 | 0.041692 | 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":12122078,"numValue":-0.0178509294057198,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122079,"numValue":0.0416915190850197,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,604 | train | mutant | 476,737 | 358 | 478,089 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48P | S48P | 1 | 1 | 0 | 0 | 48 | S | P | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,391 | MegaScale | null | null | null | null | 0.805701 | null | null | null | null | null | null | -0.231833 | -1.519625 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367056,"numValue":-0.2318327966680501,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367057,"numValue":-1.519624923174575,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367058,"numValue":0.8057006482859033,"references":[],"strValue":null,"... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,605 | train | mutant | 476,737 | 358 | 478,089 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48P | S48P | 1 | 1 | 0 | 0 | 48 | S | P | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,706 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.829682 | 0.068485 | 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":12122094,"numValue":-0.829681500385828,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122095,"numValue":0.0684850931184434,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,606 | train | mutant | 476,738 | 358 | 478,090 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48C | S48C | 1 | 1 | 0 | 0 | 48 | S | C | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,392 | MegaScale | null | null | null | null | 4.674701 | null | null | null | null | null | null | 2.229678 | 1.089178 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367059,"numValue":2.229678297891355,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367060,"numValue":1.0891784750288305,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367061,"numValue":4.674701021254192,"references":[],"strValue":null,"typ... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,607 | train | mutant | 476,738 | 358 | 478,090 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | S48C | S48C | 1 | 1 | 0 | 0 | 48 | S | C | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,695 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.013611 | 0.092952 | 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":12122072,"numValue":-0.0136114563417995,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122073,"numValue":0.0929520416356491,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,608 | train | mutant | 476,739 | 358 | 478,091 | 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 | insG48 | insG48 | 1 | 0 | 0 | 1 | 48 | - | G | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,393 | MegaScale | null | null | null | null | 1.634426 | null | null | null | null | null | null | 0.163075 | -0.812261 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367062,"numValue":0.1630746538877954,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367063,"numValue":-0.8122614452637358,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367064,"numValue":1.6344264304852372,"references":[],"strValue":null,"... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,609 | train | mutant | 476,740 | 358 | 478,092 | 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 | insA48 | insA48 | 1 | 0 | 0 | 1 | 48 | - | A | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 502,394 | MegaScale | null | null | null | null | 2.491867 | null | null | null | null | null | null | 0.745635 | -0.288716 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367065,"numValue":0.7456350114041825,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367066,"numValue":-0.2887160743392019,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367067,"numValue":2.491866638903625,"references":[],"strValue":null,"t... | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,611 | train | mutant | 476,741 | 358 | 478,093 | 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 | delS48 | delS48 | 1 | 0 | 1 | 0 | 48 | S | - | 4 | CONSERVATION | 1CSP | 247 | null | 48 | A | E | false | false | 28.590339 | 27.805 | 5,064,693 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.042326 | 0.101949 | 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":12122068,"numValue":-1.0423260661413,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122069,"numValue":0.10194871623763,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,612 | train | mutant | 476,742 | 358 | 286,809 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49Q | F49Q | 1 | 1 | 0 | 0 | 49 | F | Q | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,396 | MegaScale | null | null | null | null | 0.363703 | null | null | null | null | null | null | -0.487743 | -1.517312 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367071,"numValue":-0.4877429397135638,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367072,"numValue":-1.517311919897048,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367073,"numValue":0.3637032293110125,"references":[],"strValue":null,"... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,613 | train | mutant | 476,742 | 358 | 286,809 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49Q | F49Q | 1 | 1 | 0 | 0 | 49 | F | Q | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,081 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.734454 | 0.151032 | 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":12122844,"numValue":-0.734453747391807,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122845,"numValue":0.151031902586821,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,614 | train | mutant | 476,743 | 358 | 286,810 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49E | F49E | 1 | 1 | 0 | 0 | 49 | F | E | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,397 | MegaScale | null | null | null | null | -0.044301 | null | null | null | null | null | null | -0.517449 | -1.768303 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367074,"numValue":-0.5174494703330813,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367075,"numValue":-1.7683027577862591,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367076,"numValue":-0.0443007365562899,"references":[],"strValue":null... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,615 | train | mutant | 476,743 | 358 | 286,810 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49E | F49E | 1 | 1 | 0 | 0 | 49 | F | E | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,064,713 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.744713 | 0.106441 | 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":12122108,"numValue":-0.744713125002568,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122109,"numValue":0.106441134714102,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,616 | train | mutant | 476,744 | 358 | 286,811 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49N | F49N | 1 | 1 | 0 | 0 | 49 | F | N | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,398 | MegaScale | null | null | null | null | 0.462158 | null | null | null | null | null | null | -0.372223 | -1.479914 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367077,"numValue":-0.3722227027090012,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367078,"numValue":-1.47991404061488,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367079,"numValue":0.46215811217248,"references":[],"strValue":null,"typ... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,617 | train | mutant | 476,744 | 358 | 286,811 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49N | F49N | 1 | 1 | 0 | 0 | 49 | F | N | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,065,079 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.021454 | 0.160706 | 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":12122840,"numValue":-1.02145442017508,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122841,"numValue":0.160705776582591,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,618 | train | mutant | 476,745 | 358 | 286,812 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49H | F49H | 1 | 1 | 0 | 0 | 49 | F | H | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,399 | MegaScale | null | null | null | null | 1.444267 | null | null | null | null | null | null | 0.37509 | -0.981276 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367080,"numValue":0.3750897156319267,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367081,"numValue":-0.981275781808976,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367082,"numValue":1.444267124331533,"references":[],"strValue":null,"ty... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,620 | train | mutant | 476,746 | 358 | 286,813 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49D | F49D | 1 | 1 | 0 | 0 | 49 | F | D | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,400 | MegaScale | null | null | null | null | 0.040193 | null | null | null | null | null | null | -0.453674 | -1.716063 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367083,"numValue":-0.4536740517363103,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367084,"numValue":-1.7160627258302596,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367085,"numValue":0.0401927748459004,"references":[],"strValue":null,... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,621 | train | mutant | 476,746 | 358 | 286,813 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49D | F49D | 1 | 1 | 0 | 0 | 49 | F | D | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 5,064,712 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.823157 | 0.154672 | 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":12122106,"numValue":-0.823156625038419,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122107,"numValue":0.15467231700758,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,622 | train | mutant | 476,747 | 358 | 286,814 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F49R | F49R | 1 | 1 | 0 | 0 | 49 | F | R | 6 | CONSERVATION | 1CSP | 247 | null | 49 | A | E | false | false | 0 | 19.59 | 502,401 | MegaScale | null | null | null | null | -0.229046 | null | null | null | null | null | null | -0.891597 | -1.747563 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2367086,"numValue":-0.8915969462740863,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2367087,"numValue":-1.7475631607977735,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2367088,"numValue":-0.229046100141151,"references":[],"strValue":null,... | [{"id":20857,"numValue":6.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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