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:18965 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,965 | train | mutant | 476,213 | 358 | 477,565 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | Q23F | Q23F | 1 | 1 | 0 | 0 | 23 | Q | F | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 5,064,482 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.127243 | 0.048854 | 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":12121646,"numValue":-0.127243073487941,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121647,"numValue":0.0488536708948337,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,966 | train | mutant | 476,214 | 358 | 477,566 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | Q23P | Q23P | 1 | 1 | 0 | 0 | 23 | Q | P | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 501,841 | MegaScale | null | null | null | null | 4.550373 | null | null | null | null | null | null | 1.964117 | 1.169292 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365407,"numValue":1.9641166978066944,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365408,"numValue":1.1692919970878315,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365409,"numValue":4.550372597993022,"references":[],"strValue":null,"ty... | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,967 | train | mutant | 476,214 | 358 | 477,566 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | Q23P | Q23P | 1 | 1 | 0 | 0 | 23 | Q | P | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 5,064,490 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.415029 | 0.046534 | 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":12121662,"numValue":-0.415028588535771,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121663,"numValue":0.0465336695552779,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18968 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,968 | train | mutant | 476,215 | 358 | 477,567 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | Q23C | Q23C | 1 | 1 | 0 | 0 | 23 | Q | C | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 501,842 | MegaScale | null | null | null | null | 4.55777 | null | null | null | null | null | null | 2.034425 | 1.021689 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365410,"numValue":2.034424683843101,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365411,"numValue":1.021688638085183,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365412,"numValue":4.557770157671339,"references":[],"strValue":null,"type... | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18969 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,969 | train | mutant | 476,215 | 358 | 477,567 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | Q23C | Q23C | 1 | 1 | 0 | 0 | 23 | Q | C | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 5,064,479 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.025637 | 0.055802 | 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":12121640,"numValue":-0.0256374037324659,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121641,"numValue":0.0558019047329313,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,970 | train | mutant | 476,216 | 358 | 477,568 | 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 | insA23 | insA23 | 1 | 0 | 0 | 1 | 23 | - | A | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 501,844 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.873183 | 1.378539 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365416,"numValue":1.873183048606927,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365417,"numValue":1.3785386658524088,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365418,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18971 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,971 | train | mutant | 476,217 | 358 | 477,569 | 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 | delQ23 | delQ23 | 1 | 0 | 1 | 0 | 23 | Q | - | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 501,845 | MegaScale | null | null | null | null | 4.553269 | null | null | null | null | null | null | 1.784307 | 1.102268 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365419,"numValue":1.7843071744317576,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365420,"numValue":1.1022676499328825,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365421,"numValue":4.553268682049591,"references":[],"strValue":null,"ty... | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18972 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,972 | train | mutant | 476,217 | 358 | 477,569 | 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 | delQ23 | delQ23 | 1 | 0 | 1 | 0 | 23 | Q | - | 4 | CONSERVATION | 1CSP | 247 | null | 23 | A | S | false | false | 102.870499 | 58.305555 | 5,064,477 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.040787 | 0.08008 | 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":12121636,"numValue":-1.04078745390754,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121637,"numValue":0.0800797330064261,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20831,"numValue":4.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,973 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,090 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:D24K | 48.7 | null | null | null | null | null | 32.27 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PoPMuSiC-2.0_S2648.csv|M47andM8_S1810.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:D24K","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7818,"numValue":48.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUT... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18974 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,974 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,135 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:D24K | 50.9 | null | null | null | null | null | 34.18 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|EASE-MM_S238.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7953,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7954,"numValue":34.18,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,975 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,181 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:D24K | 52.3 | null | null | null | null | null | 35.37 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8091,"numValue":52.3,"references":[],"strValue":null,"type":"TM"}... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18976 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,976 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,227 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:D24K | 54 | null | null | null | null | null | 36.81 | 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":8229,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8230,"numValue":36.81,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8231,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18977 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,977 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,273 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:D24K | 57.2 | null | null | null | null | null | 39.44 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8367,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8368,"numValue":39.44,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18978 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,978 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,319 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:D24K | 60.7 | null | null | null | null | null | 42.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8505,"numValue":60.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PO... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,979 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 7,251 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:D24K | null | null | 0.26 | 0.36 | 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":[],"id":25340,"numValue":0.26,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25341,"numValue":0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25342,"numValue":null,"references":[],"strValue":"Unknown"... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18980 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,980 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 7,283 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:D24K | null | null | 0.69 | 0.41 | 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":25436,"numValue":0.69,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25437,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25438,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18981 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,981 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,851 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.729908 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365437,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365438,"numValue":1.7299084142273076,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365439,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18982 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,982 | train | mutant | 1,172 | 358 | 1,318 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24K | D24K | 1 | 1 | 0 | 0 | 24 | D | K | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,358 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.046962 | 0.065959 | 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":12123398,"numValue":0.0469617324380964,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123399,"numValue":0.06595913508616,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18983 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,983 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,091 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:D24N | 46.5 | null | null | null | null | null | 29.4 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PON-TStab_dataset.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.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:D24N","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7821,"numValue":46.5,"references":[],"strValue":null,"type":"T... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18984 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,984 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,136 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:D24N | 48.4 | null | null | null | null | null | 31.07 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7956,"numValue":48.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7957,"numValue":31.07,"references":[],"strValue":null,"type":"DHVH"},{"... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18986 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,986 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,228 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:D24N | 51.3 | null | null | null | null | null | 33.46 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8232,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8233,"numValue":33.46,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8234,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18987 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,987 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,274 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:D24N | 55.7 | null | null | null | null | null | 37.05 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8370,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8371,"numValue":37.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18988 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,988 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 2,320 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:D24N | 60.6 | null | null | null | null | null | 41.11 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S2204.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv|iPTREE-STAB_S1859.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S2204.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":8508,"numValue":60.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOM... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18989 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,989 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 7,252 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:D24N | null | null | 0.07 | 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":25343,"numValue":0.07,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25344,"numValue":0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25345,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18990 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,990 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 7,284 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:D24N | null | null | 0.65 | 0.45 | 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":25439,"numValue":0.65,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25440,"numValue":0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25441,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18991 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,991 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,848 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.746111 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365428,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365429,"numValue":1.7461107945162315,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365430,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18992 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,992 | train | mutant | 1,173 | 358 | 1,319 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24N | D24N | 1 | 1 | 0 | 0 | 24 | D | N | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,361 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.009181 | 0.06388 | 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":12123404,"numValue":0.00918123152399073,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123405,"numValue":0.063879695628896,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18993 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,993 | train | mutant | 476,218 | 358 | 477,570 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24Q | D24Q | 1 | 1 | 0 | 0 | 24 | D | Q | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,846 | 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":2365422,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365423,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365424,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18994 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,994 | train | mutant | 476,218 | 358 | 477,570 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24Q | D24Q | 1 | 1 | 0 | 0 | 24 | D | Q | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,363 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.031429 | 0.056675 | 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":12123408,"numValue":-0.0314286515145168,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123409,"numValue":0.0566749098820633,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18995 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,995 | train | mutant | 476,219 | 358 | 477,571 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24E | D24E | 1 | 1 | 0 | 0 | 24 | D | E | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,847 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.709569 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365425,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365426,"numValue":1.7095686028226127,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365427,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18996 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,996 | train | mutant | 476,219 | 358 | 477,571 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24E | D24E | 1 | 1 | 0 | 0 | 24 | D | E | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,353 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.033839 | 0.054071 | 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":12123388,"numValue":-0.0338385024503013,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123389,"numValue":0.0540706945627102,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18997 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,997 | train | mutant | 476,220 | 358 | 477,572 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24H | D24H | 1 | 1 | 0 | 0 | 24 | D | H | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,849 | 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":2365431,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365432,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365433,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18998 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,998 | train | mutant | 476,220 | 358 | 477,572 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24H | D24H | 1 | 1 | 0 | 0 | 24 | D | H | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,356 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.028724 | 0.105295 | 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":12123394,"numValue":-0.0287243927270711,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123395,"numValue":0.105295090816542,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18999 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,999 | train | mutant | 476,221 | 358 | 477,573 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24R | D24R | 1 | 1 | 0 | 0 | 24 | D | R | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,850 | 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":2365434,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365435,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365436,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19000 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,000 | train | mutant | 476,221 | 358 | 477,573 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24R | D24R | 1 | 1 | 0 | 0 | 24 | D | R | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,364 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.000658 | 0.034453 | 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":12123410,"numValue":0.000657510868709872,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123411,"numValue":0.0344528335007676,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19001 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,001 | train | mutant | 476,222 | 358 | 477,574 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24T | D24T | 1 | 1 | 0 | 0 | 24 | D | T | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,852 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.589897 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365440,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365441,"numValue":1.5898966972457826,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365442,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19002 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,002 | train | mutant | 476,222 | 358 | 477,574 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24T | D24T | 1 | 1 | 0 | 0 | 24 | D | T | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,366 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.054261 | 0.04188 | 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":12123414,"numValue":-0.0542612071102194,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123415,"numValue":0.0418798235736415,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19003 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,003 | train | mutant | 476,223 | 358 | 477,575 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24S | D24S | 1 | 1 | 0 | 0 | 24 | D | S | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,853 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.731535 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365443,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365444,"numValue":1.7315353433330114,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365445,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19004 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,004 | train | mutant | 476,223 | 358 | 477,575 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24S | D24S | 1 | 1 | 0 | 0 | 24 | D | S | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,365 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.041083 | 0.037634 | 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":12123412,"numValue":-0.041083388999929,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123413,"numValue":0.0376344071512158,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19005 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,005 | train | mutant | 476,224 | 358 | 477,576 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24A | D24A | 1 | 1 | 0 | 0 | 24 | D | A | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,854 | 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":2365446,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365447,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365448,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19006 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,006 | train | mutant | 476,224 | 358 | 477,576 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24A | D24A | 1 | 1 | 0 | 0 | 24 | D | A | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,064,492 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.111686 | 0.04565 | 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":12121666,"numValue":-0.111686071926414,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121667,"numValue":0.0456498571845912,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19008 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,008 | train | mutant | 476,225 | 358 | 477,577 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24G | D24G | 1 | 1 | 0 | 0 | 24 | D | G | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,355 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.054654 | 0.045553 | 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":12123392,"numValue":-0.0546537509124343,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123393,"numValue":0.0455525492561203,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19009 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,009 | train | mutant | 476,226 | 358 | 477,578 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24M | D24M | 1 | 1 | 0 | 0 | 24 | D | M | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,856 | 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":2365452,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365453,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365454,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19010 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,010 | train | mutant | 476,226 | 358 | 477,578 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24M | D24M | 1 | 1 | 0 | 0 | 24 | D | M | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,360 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.083945 | 0.039783 | 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":12123402,"numValue":-0.083945492103644,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123403,"numValue":0.0397828729827005,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19011 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,011 | train | mutant | 476,227 | 358 | 477,579 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24L | D24L | 1 | 1 | 0 | 0 | 24 | D | L | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,857 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.157025 | 1.705041 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365455,"numValue":2.1570245737099683,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365456,"numValue":1.7050407046903038,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365457,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19013 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,013 | train | mutant | 476,228 | 358 | 477,580 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24V | D24V | 1 | 1 | 0 | 0 | 24 | D | V | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,858 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.681195 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365458,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365459,"numValue":1.681195030401136,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365460,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19014 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,014 | train | mutant | 476,228 | 358 | 477,580 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24V | D24V | 1 | 1 | 0 | 0 | 24 | D | V | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,367 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.097447 | 0.045855 | 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":12123416,"numValue":-0.0974471588507616,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123417,"numValue":0.0458550778576898,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19015 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,015 | train | mutant | 476,229 | 358 | 477,581 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24I | D24I | 1 | 1 | 0 | 0 | 24 | D | I | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,859 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.675831 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365461,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365462,"numValue":1.6758305454413631,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365463,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19016 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,016 | train | mutant | 476,229 | 358 | 477,581 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24I | D24I | 1 | 1 | 0 | 0 | 24 | D | I | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,357 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.267292 | 0.060937 | 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":12123396,"numValue":-0.26729166182376,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123397,"numValue":0.060937224088475,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19018 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,018 | train | mutant | 476,230 | 358 | 477,582 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24W | D24W | 1 | 1 | 0 | 0 | 24 | D | W | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,368 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.296014 | 0.051357 | 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":12123418,"numValue":-0.296014214501758,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123419,"numValue":0.0513568307191041,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19019 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,019 | train | mutant | 476,231 | 358 | 477,583 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24Y | D24Y | 1 | 1 | 0 | 0 | 24 | D | Y | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,861 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.231932 | 1.670293 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365467,"numValue":2.2319323468844807,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365468,"numValue":1.6702928138759543,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365469,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19020 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,020 | train | mutant | 476,231 | 358 | 477,583 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24Y | D24Y | 1 | 1 | 0 | 0 | 24 | D | Y | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,369 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.1558 | 0.059159 | 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":12123420,"numValue":-0.15580002174938,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123421,"numValue":0.0591592644048088,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19021 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,021 | train | mutant | 476,232 | 358 | 477,584 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24F | D24F | 1 | 1 | 0 | 0 | 24 | D | F | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,862 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.030134 | 1.637107 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365470,"numValue":2.0301342570557392,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365471,"numValue":1.6371070939165484,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365472,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19022 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,022 | train | mutant | 476,232 | 358 | 477,584 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24F | D24F | 1 | 1 | 0 | 0 | 24 | D | F | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,354 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.284572 | 0.05943 | 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":12123390,"numValue":-0.284572176016886,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123391,"numValue":0.0594304385701764,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19023 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,023 | train | mutant | 476,233 | 358 | 477,585 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24P | D24P | 1 | 1 | 0 | 0 | 24 | D | P | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,863 | 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":2365473,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365474,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365475,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19024 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,024 | train | mutant | 476,233 | 358 | 477,585 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24P | D24P | 1 | 1 | 0 | 0 | 24 | D | P | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,065,362 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.002694 | 0.055039 | 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":12123406,"numValue":-0.00269383184269936,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123407,"numValue":0.0550389038508731,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19025 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,025 | train | mutant | 476,234 | 358 | 477,586 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24C | D24C | 1 | 1 | 0 | 0 | 24 | D | C | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,864 | MegaScale | null | null | null | null | 4.788367 | null | null | null | null | null | null | 1.974453 | 1.09725 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365476,"numValue":1.9744530958368516,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365477,"numValue":1.097250299559565,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365478,"numValue":4.7883665635448445,"references":[],"strValue":null,"ty... | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19026 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,026 | train | mutant | 476,234 | 358 | 477,586 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D24C | D24C | 1 | 1 | 0 | 0 | 24 | D | C | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,064,493 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.040147 | 0.079233 | 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":12121668,"numValue":-0.040146804021832,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121669,"numValue":0.0792325130783021,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19027 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,027 | train | mutant | 476,235 | 358 | 477,587 | 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 | insG24 | insG24 | 1 | 0 | 0 | 1 | 24 | - | G | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,865 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.869183 | 1.349383 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365479,"numValue":1.869182524729923,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365480,"numValue":1.3493832985531888,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365481,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19028 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,028 | train | mutant | 476,236 | 358 | 477,588 | 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 | insA24 | insA24 | 1 | 0 | 0 | 1 | 24 | - | A | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,866 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.905747 | 1.44994 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365482,"numValue":1.9057466307125737,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365483,"numValue":1.4499399476933024,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365484,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19029 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,029 | train | mutant | 476,237 | 358 | 477,589 | 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 | delD24 | delD24 | 1 | 0 | 1 | 0 | 24 | D | - | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,867 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.911167 | 1.36351 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365485,"numValue":1.9111672663051933,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365486,"numValue":1.3635104513966314,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365487,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19030 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,030 | train | mutant | 476,237 | 358 | 477,589 | 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 | delD24 | delD24 | 1 | 0 | 1 | 0 | 24 | D | - | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 501,889 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.869007 | 1.359499 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365551,"numValue":1.8690074662060887,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365552,"numValue":1.359498581829768,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365553,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19031 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,031 | train | mutant | 476,237 | 358 | 477,589 | 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 | delD24 | delD24 | 1 | 0 | 1 | 0 | 24 | D | - | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,064,491 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.034082 | 0.086636 | 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":12121664,"numValue":-1.03408156066584,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121665,"numValue":0.0866358891880741,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19032 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,032 | train | mutant | 476,237 | 358 | 477,589 | 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 | delD24 | delD24 | 1 | 0 | 1 | 0 | 24 | D | - | 1 | CONSERVATION | 1CSP | 247 | null | 24 | A | L | false | false | 123.0179 | 52.48 | 5,064,494 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.028944 | 0.079089 | 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":12121670,"numValue":-1.02894359777312,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121671,"numValue":0.0790889279156482,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20832,"numValue":1.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19033 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,033 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,092 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:D25K | 36.3 | null | null | null | null | null | 18.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"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:D25K","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7824,"numValue":36.3,"references":[],"... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19034 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,034 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,137 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:D25K | 39.4 | null | null | null | null | null | 20.79 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.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":["M47andM8_S2760.csv"],"id":7959,"numValue":39.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv"],"id":7960,"numValue":20.79,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["M47andM8_S2760.csv"],"id":7961,"numValue":null,"references":[],"strValue... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19035 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,035 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,183 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:D25K | 40.9 | null | null | null | null | null | 21.99 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8097,"numValue":40.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8098,"numValue":21.99,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8099,"numValue":null,"referenc... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19036 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,036 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,229 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:D25K | 43.5 | null | null | null | null | null | 24.14 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8235,"numValue":43.5,"references":[],"strValue":null,"ty... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19037 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,037 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,275 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:D25K | 49.5 | null | null | null | null | null | 29.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8373,"numValue":49.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8374,"numValue":29.16,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19039 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,039 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 7,285 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:D25K | null | null | 0.02 | 1.08 | 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":25442,"numValue":0.02,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25443,"numValue":1.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25444,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19040 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,040 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,873 | MegaScale | null | null | null | null | 4.481762 | null | null | null | null | null | null | 1.769172 | 1.084669 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365503,"numValue":1.7691724736782568,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365504,"numValue":1.0846693978746234,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365505,"numValue":4.481762380803223,"references":[],"strValue":null,"ty... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19041 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,041 | train | mutant | 1,174 | 358 | 1,320 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25K | D25K | 1 | 1 | 0 | 0 | 25 | D | K | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,341 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.583707 | 0.05106 | 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":12123364,"numValue":-0.58370656173153,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123365,"numValue":0.0510599388011945,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19042 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,042 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,093 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:D25Q | 42.9 | null | null | null | null | null | 27.96 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|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|_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:D25Q","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7827,"numValue":... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:19043 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,043 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,138 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:D25Q | 44.2 | null | null | null | null | null | 29.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | M47andM8_S2760.csv|STRUM_Q3421.csv|M47andM8_S1810.csv|EASE-MM_S238.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["M47andM8_S2760.csv","STRUM_Q3421.csv"],"id":7962,"numValue":44.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":7963,"numValue":29.16,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["EASE-MM_S238.csv","M47andM8_S2760.csv"],"id":7964,"... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19044 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,044 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,184 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:D25Q | 45.5 | null | null | null | null | null | 30.11 | 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":8100,"numValue":45.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S238.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":8101,"numValue":30.11,"references":[],"strValue":null,"type... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19045 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,045 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,230 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:D25Q | 47.3 | null | null | null | null | null | 31.55 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":8238,"numValue":47.3,"references":[],"strValue":null,"ty... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19046 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,046 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,276 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:D25Q | 51 | null | null | null | null | null | 34.66 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8376,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8377,"numValue":34.66,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":8... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19047 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,047 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 2,322 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:D25Q | 60.5 | null | null | null | null | null | 42.78 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19048 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,048 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 7,286 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:D25Q | null | null | 0.67 | 0.41 | 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":25445,"numValue":0.67,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25446,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25447,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:19049 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,049 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,868 | MegaScale | null | null | null | null | 4.894515 | null | null | null | null | null | null | 2.117957 | 1.245646 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365488,"numValue":2.117956966202088,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365489,"numValue":1.24564587507835,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365490,"numValue":4.894515089756468,"references":[],"strValue":null,"type"... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19050 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,050 | train | mutant | 1,175 | 358 | 1,321 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25Q | D25Q | 1 | 1 | 0 | 0 | 25 | D | Q | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,346 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.254814 | 0.057762 | 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":12123374,"numValue":-0.254814289060546,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123375,"numValue":0.0577622194132169,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19051 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,051 | train | mutant | 476,238 | 358 | 477,590 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25E | D25E | 1 | 1 | 0 | 0 | 25 | D | E | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,869 | MegaScale | null | null | null | null | 4.897739 | null | null | null | null | null | null | 2.132611 | 1.320257 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365491,"numValue":2.1326110978219988,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365492,"numValue":1.32025706373817,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365493,"numValue":4.8977393772823135,"references":[],"strValue":null,"typ... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19052 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,052 | train | mutant | 476,238 | 358 | 477,590 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25E | D25E | 1 | 1 | 0 | 0 | 25 | D | E | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,336 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.14763 | 0.038726 | 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":12123354,"numValue":-0.147629590516093,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123355,"numValue":0.038725752523336,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19053 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,053 | train | mutant | 476,239 | 358 | 477,591 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25N | D25N | 1 | 1 | 0 | 0 | 25 | D | N | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,870 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.536335 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365494,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365495,"numValue":1.5363349503896455,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365496,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19055 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,055 | train | mutant | 476,240 | 358 | 477,592 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25H | D25H | 1 | 1 | 0 | 0 | 25 | D | H | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,871 | MegaScale | null | null | null | null | 4.83604 | null | null | null | null | null | null | 2.020243 | 1.234808 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365497,"numValue":2.020242982274784,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365498,"numValue":1.23480750215126,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365499,"numValue":4.836039879816534,"references":[],"strValue":null,"type"... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19056 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,056 | train | mutant | 476,240 | 358 | 477,592 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25H | D25H | 1 | 1 | 0 | 0 | 25 | D | H | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,339 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.343518 | 0.075064 | 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":12123360,"numValue":-0.343518148066663,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123361,"numValue":0.0750644952533788,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19057 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,057 | train | mutant | 476,241 | 358 | 477,593 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25R | D25R | 1 | 1 | 0 | 0 | 25 | D | R | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,872 | MegaScale | null | null | null | null | 4.484916 | null | null | null | null | null | null | 2.144884 | 0.957828 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365500,"numValue":2.1448842218379687,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365501,"numValue":0.9578275544639676,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365502,"numValue":4.484915963854451,"references":[],"strValue":null,"ty... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19058 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,058 | train | mutant | 476,241 | 358 | 477,593 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25R | D25R | 1 | 1 | 0 | 0 | 25 | D | R | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,347 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.558173 | 0.0342 | 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":12123376,"numValue":-0.558172998101744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123377,"numValue":0.0341999187556999,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19059 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,059 | train | mutant | 476,242 | 358 | 477,594 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25T | D25T | 1 | 1 | 0 | 0 | 25 | D | T | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,874 | MegaScale | null | null | null | null | 4.852352 | null | null | null | null | null | null | null | 1.214439 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365506,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2365507,"numValue":1.214438846611177,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365508,"numValue":4.852351884926176,"references":[],"strValue":null,"type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19060 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,060 | train | mutant | 476,242 | 358 | 477,594 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25T | D25T | 1 | 1 | 0 | 0 | 25 | D | T | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,349 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.38507 | 0.040927 | 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":12123380,"numValue":-0.385070136230487,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123381,"numValue":0.0409265922849319,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19061 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,061 | train | mutant | 476,243 | 358 | 477,595 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25S | D25S | 1 | 1 | 0 | 0 | 25 | D | S | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,875 | MegaScale | null | null | null | null | 4.968405 | null | null | null | null | null | null | 2.15486 | 1.275965 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365509,"numValue":2.15486009296921,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365510,"numValue":1.2759645946654774,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365511,"numValue":4.968405047095225,"references":[],"strValue":null,"type... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19063 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,063 | train | mutant | 476,244 | 358 | 477,596 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25A | D25A | 1 | 1 | 0 | 0 | 25 | D | A | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,876 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.236539 | 1.299177 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365512,"numValue":2.23653874160017,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365513,"numValue":1.2991770055524996,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365514,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19064 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,064 | train | mutant | 476,244 | 358 | 477,596 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25A | D25A | 1 | 1 | 0 | 0 | 25 | D | A | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,064,495 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.218952 | 0.035219 | 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":12121672,"numValue":-0.218951732630075,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121673,"numValue":0.035218937932262,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19066 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,066 | train | mutant | 476,245 | 358 | 477,597 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25G | D25G | 1 | 1 | 0 | 0 | 25 | D | G | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,338 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.512759 | 0.033548 | 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":12123358,"numValue":-0.512759053608787,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123359,"numValue":0.0335476029588725,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19067 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,067 | train | mutant | 476,246 | 358 | 477,598 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25M | D25M | 1 | 1 | 0 | 0 | 25 | D | M | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,878 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.169177 | 1.439234 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365518,"numValue":2.1691766200572715,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365519,"numValue":1.439233875139962,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365520,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19068 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,068 | train | mutant | 476,246 | 358 | 477,598 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25M | D25M | 1 | 1 | 0 | 0 | 25 | D | M | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,343 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.490997 | 0.042838 | 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":12123368,"numValue":-0.490997406573502,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123369,"numValue":0.0428378451234376,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19069 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,069 | train | mutant | 476,247 | 358 | 477,599 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25L | D25L | 1 | 1 | 0 | 0 | 25 | D | L | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,879 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.110483 | 1.420947 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365521,"numValue":2.110483161615748,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365522,"numValue":1.4209466992476771,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365523,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:19070 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,070 | train | mutant | 476,247 | 358 | 477,599 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25L | D25L | 1 | 1 | 0 | 0 | 25 | D | L | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,342 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.441766 | 0.02755 | 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":12123366,"numValue":-0.44176634161382,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123367,"numValue":0.0275495275275328,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19071 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,071 | train | mutant | 476,248 | 358 | 477,600 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25V | D25V | 1 | 1 | 0 | 0 | 25 | D | V | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 501,880 | MegaScale | null | null | null | null | 4.920425 | null | null | null | null | null | null | 2.032832 | 1.277655 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2365524,"numValue":2.032831625283456,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2365525,"numValue":1.2776545844248646,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2365526,"numValue":4.920424665265457,"references":[],"strValue":null,"typ... | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:19072 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19,072 | train | mutant | 476,248 | 358 | 477,600 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | D25V | D25V | 1 | 1 | 0 | 0 | 25 | D | V | 9 | CONSERVATION | 1CSP | 247 | null | 25 | A | L | false | false | 59.869746 | 36.8375 | 5,065,350 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.667332 | 0.034181 | 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":12123382,"numValue":-0.667332375976246,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123383,"numValue":0.0341813955950329,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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