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:1772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,772 | train | mutant | 1,778 | 41 | 1,991 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | H31N | H31N | 1 | 1 | 0 | 0 | 31 | H | N | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 31 | A | E | true | true | 34.538017 | 15.907 | 3,420 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:H31N | 55 | -11 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 303 | ARTICLE | pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. | 1,990 | 10.1021/bi00461a025 | 2337607 | Biochemistry;29;2403-8 | 3 | Anderson D E|Becktel W J|Dahlquist F W | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12619,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":12620,"numV... | [{"id":6822,"numValue":9.0,"position":31,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,773 | train | mutant | 1,778 | 41 | 1,991 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | H31N | H31N | 1 | 1 | 0 | 0 | 31 | H | N | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 31 | A | E | true | true | 34.538017 | 15.907 | 6,756 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | 66 | KCl | 0.15 M | 2LZM_A:H31N | null | null | null | 4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 303 | ARTICLE | pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. | 1,990 | 10.1021/bi00461a025 | 2337607 | Biochemistry;29;2403-8 | 3 | Anderson D E|Becktel W J|Dahlquist F W | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":66.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23982,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23983,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6822,"numValue":9.0,"position":31,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,774 | train | mutant | 6,883 | 41 | 7,525 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | H31N|D70N | H31N|D70N | 2 | 2 | 0 | 0 | 31 | H | N | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 31|70 | A | E|H | true | true | 32.854148 | 15.490687 | 14,713 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:H31N 2LZM_A:D70N | 55 | -11 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 303 | ARTICLE | pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. | 1,990 | 10.1021/bi00461a025 | 2337607 | Biochemistry;29;2403-8 | 3 | Anderson D E|Becktel W J|Dahlquist F W | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":54404,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54405,"numValue":-11.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54406,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6822,"numValue":9.0,"position":31,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6861,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,777 | train | mutant | 7,380 | 41 | 8,050 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L32A|L33A|T34A|E108V | L32A|L33A|T34A|E108V | 4 | 4 | 0 | 0 | 32 | L | A | 9 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 32|33|34|108 | A | E|H | true | true | 40.580171 | 27.706225 | 16,790 | ProTherm | 3.05 | CD | Thermal | glycine-HCl | 20 mM | 51.6 | 2LZM_A:L32A 2LZM_A:L33A 2LZM_A:T34A 2LZM_A:E108V | null | null | null | 3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 164 | ARTICLE | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation. | 2,004 | 10.1110/ps.04875504 | 15340171 | Protein Sci;13;2716-24 | 5 | Baase Walter A|Matthews Brian W|He Molly M|Wood Zachary A|Xiao Hong | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":51.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFE... | [{"datasets":[],"id":61705,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61706,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61707,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20,"numValue":null,"position":32,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6823,"numValue":9.0,"position":32,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":n... | |||||||||||||
fireprotdb:1778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,778 | train | mutant | 1,125 | 41 | 1,269 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L33A | L33A | 1 | 1 | 0 | 0 | 33 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 33 | A | E | false | true | 17.009017 | 18.881875 | 2,019 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L33A | 56.5 | -8.8 | null | null | null | null | 83 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|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 | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"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":7537,"numValue":56.5,"references":[],"strValue":null,"type":"TM"}... | [{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,779 | train | mutant | 1,125 | 41 | 1,269 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L33A | L33A | 1 | 1 | 0 | 0 | 33 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 33 | A | E | false | true | 17.009017 | 18.881875 | 3,142 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L33A | 39.4 | -12.3 | null | null | null | 1.8 | 67 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11462,"numValue":39.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11463,"numValue":-12.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11464,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,780 | train | mutant | 1,125 | 41 | 1,269 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L33A | L33A | 1 | 1 | 0 | 0 | 33 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 33 | A | E | false | true | 17.009017 | 18.881875 | 6,786 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:L33A | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24060,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24061,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24062,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1781 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,781 | train | mutant | 1,125 | 41 | 1,269 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L33A | L33A | 1 | 1 | 0 | 0 | 33 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 33 | A | E | false | true | 17.009017 | 18.881875 | 7,576 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:L33A | null | null | null | 3.6 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26201,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26202,"numValue":3.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26203,"numV... | [{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,782 | train | mutant | 1,139 | 41 | 1,283 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L33M | L33M | 1 | 1 | 0 | 0 | 33 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 33 | A | E | false | true | 17.009017 | 18.881875 | 2,039 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L33M | 60 | -5.3 | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7637,"numValue":60.0,"references":[],... | [{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,783 | train | mutant | 1,139 | 41 | 1,283 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L33M | L33M | 1 | 1 | 0 | 0 | 33 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 33 | A | E | false | true | 17.009017 | 18.881875 | 6,806 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:L33M | null | null | null | 2 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|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 | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24120,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24121,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24122,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6824,"numValue":7.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,784 | train | mutant | 7,396 | 41 | 8,079 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37A | T34A|K35A|S36A|P37A | 4 | 4 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37 | A | E|S | true | true | 80.053812 | 37.885219 | 15,790 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37A | 51.8 | -1.6 | null | null | null | 1.8 | 109 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57978,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57979,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57980,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57981,"numValue":109.0,"references":[... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,785 | train | mutant | 7,396 | 41 | 8,079 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37A | T34A|K35A|S36A|P37A | 4 | 4 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37 | A | E|S | true | true | 80.053812 | 37.885219 | 16,782 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37A | null | null | null | 0.7 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61681,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61682,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61683,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1786 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,786 | train | mutant | 7,397 | 41 | 8,080 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37A|S38A|N40A|S44A|E45A|D47A|K48A | T34A|K35A|S36A|P37A|S38A|N40A|S44A|E45A|D47A|K48A | 10 | 10 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|38|40|44|45|47|48 | A | E|S|L|H | true | true | 78.875389 | 32.557782 | 15,791 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37A 2LZM_A:S38A 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A | 41.7 | -10 | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57983,"numValue":41.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57984,"numValue":-10.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57985,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57986,"numValue":null,"references":[... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,787 | train | mutant | 7,398 | 41 | 8,081 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37A|S38D|N40A|S44A|E45A|D47A|K48A | T34A|K35A|S36A|P37A|S38D|N40A|S44A|E45A|D47A|K48A | 10 | 10 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|38|40|44|45|47|48 | A | E|S|L|H | true | true | 78.875389 | 32.557782 | 15,792 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37A 2LZM_A:S38D 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A | 47.9 | -3.8 | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57987,"numValue":47.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57988,"numValue":-3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57989,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57990,"numValue":null,"references":[]... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,788 | train | mutant | 7,399 | 41 | 8,082 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35D|S36A|P37A|S38A|N40A|S44A|E45A|D47A|K48A | T34A|K35D|S36A|P37A|S38A|N40A|S44A|E45A|D47A|K48A | 10 | 10 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|38|40|44|45|47|48 | A | E|S|L|H | true | true | 78.875389 | 32.557782 | 15,793 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35D 2LZM_A:S36A 2LZM_A:P37A 2LZM_A:S38A 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A | 42.5 | -9.2 | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57991,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57992,"numValue":-9.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57993,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57994,"numValue":null,"references":[]... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,789 | train | mutant | 7,400 | 41 | 8,083 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36D|P37A|S38A|N40A|S44A|E45A|D47A|K48A | T34A|K35A|S36D|P37A|S38A|N40A|S44A|E45A|D47A|K48A | 10 | 10 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|38|40|44|45|47|48 | A | E|S|L|H | true | true | 78.875389 | 32.557782 | 15,794 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36D 2LZM_A:P37A 2LZM_A:S38A 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A | 43.2 | -8.5 | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57995,"numValue":43.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57996,"numValue":-8.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57997,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57998,"numValue":null,"references":[]... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,790 | train | mutant | 7,401 | 41 | 8,084 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37D|S38A|N40A|S44A|E45A|D47A|K48A | T34A|K35A|S36A|P37D|S38A|N40A|S44A|E45A|D47A|K48A | 10 | 10 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|38|40|44|45|47|48 | A | E|S|L|H | true | true | 78.875389 | 32.557782 | 15,795 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37D 2LZM_A:S38A 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A | 44.3 | -7.4 | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57999,"numValue":44.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58000,"numValue":-7.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58001,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":58002,"numValue":null,"references":[]... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,791 | train | mutant | 7,402 | 41 | 8,085 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37A|S38A|N40D|S44A|E45A|D47A|K48A | T34A|K35A|S36A|P37A|S38A|N40D|S44A|E45A|D47A|K48A | 10 | 10 | 0 | 0 | 34 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|38|40|44|45|47|48 | A | E|S|L|H | true | true | 78.875389 | 32.557782 | 15,796 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37A 2LZM_A:S38A 2LZM_A:N40D 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A | 42 | -9.7 | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":58003,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58004,"numValue":-9.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58005,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":58006,"numValue":null,"references":[]... | [{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6827,"numValue":4.0,"position":36,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,793 | train | mutant | 7,408 | 41 | 8,091 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | T34A|K35A|S36A|P37A|E128A|V131A|N132A | T34A|K35A|S36A|P37A|E128A|V131A|N132A | 7 | 7 | 0 | 0 | 34 | T | A | 7 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 34|35|36|37|128|131|132 | A | E|S|H | true | true | 78.363853 | 32.476056 | 16,785 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:T34A 2LZM_A:K35A 2LZM_A:S36A 2LZM_A:P37A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | 0.2 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61690,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61691,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61692,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6825,"numValue":7.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6826,"numValue":5.0,"position":35,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,794 | train | mutant | 1,598 | 41 | 1,798 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P37A | P37A | 1 | 1 | 0 | 0 | 37 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 37 | A | S | true | false | 126.875582 | 45.525 | 2,996 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:P37A | 41.1 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:P37A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10879,"numValue":41.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv","Sar... | [{"id":6828,"numValue":5.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,795 | train | mutant | 1,598 | 41 | 1,798 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P37A | P37A | 1 | 1 | 0 | 0 | 37 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 37 | A | S | true | false | 126.875582 | 45.525 | 4,654 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:P37A | 41.1 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:P37A","typ... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":17208,"numValue":41.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":17209,"numValue":-0.8,"references":[],"strValue":null,"typ... | [{"id":6828,"numValue":5.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,796 | train | mutant | 1,598 | 41 | 1,798 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P37A | P37A | 1 | 1 | 0 | 0 | 37 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 37 | A | S | true | false | 126.875582 | 45.525 | 12,604 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:P37A | null | null | null | 0 | null | null | null | 6.3 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":45715,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":45716,"numValue":6.3,"references":[],"strValue":null,"type":"CM"},{"datasets":["guerios_625_map.csv"... | [{"id":6828,"numValue":5.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1797 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,797 | train | mutant | 1,598 | 41 | 1,798 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | P37A | P37A | 1 | 1 | 0 | 0 | 37 | P | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 37 | A | S | true | false | 126.875582 | 45.525 | 13,899 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:P37A | null | null | 17.9 | null | null | null | null | 2.93 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":51437,"numValue":17.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":51438,"numValue":2.93,"references":[],"strValue":null,"type":"CM"},{"datasets":["guerios_625_map.csv... | [{"id":6828,"numValue":5.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,799 | train | mutant | 503 | 41 | 553 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38N | S38N | 1 | 1 | 0 | 0 | 38 | S | N | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 823 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:S38N | 62.3 | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":3116,"numValue":62.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":3117,"numValue":-0.1,"references":[],"strValue":null,"typ... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1800 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,800 | train | mutant | 503 | 41 | 553 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38N | S38N | 1 | 1 | 0 | 0 | 38 | S | N | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 7,062 | ProTherm | 6.7 | CD | Thermal | HCl | 0.01 N | 62.4 | KCl | 200 mM | 2LZM_A:S38N | null | null | null | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24798,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24799,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,801 | train | mutant | 503 | 41 | 553 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38N | S38N | 1 | 1 | 0 | 0 | 38 | S | N | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 8,157 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 39.5 | KCl | 200 mM | 2LZM_A:S38N | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":39.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27704,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27705,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,802 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 899 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S38D | 53.88 | 0.46 | null | null | null | 1.8 | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3326,"numValue":53.88,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3327,"numValue":0.46,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3328,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,803 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 906 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S38D | 67.87 | 1.36 | null | null | null | 2.5 | 140 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3361,"numValue":67.87,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3362,"numValue":1.36,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3363,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,804 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 3,294 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:S38D | 40.6 | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":12126,"numValue":40.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12127,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12128,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,805 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 3,299 | ProTherm | 6.9 | CD | Thermal | phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:S38D | 67.6 | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.9,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":[],"id":12141,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12142,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12143,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,806 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 6,721 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:S38D | null | null | null | -0.6 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23885,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":23886,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23887,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1807 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,807 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 6,749 | ProTherm | 6.9 | CD | Thermal | phosphate | 10 mM | 66.1 | KCl | 150 mM | 2LZM_A:S38D | null | null | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.9,"strValue":null,"type":"PH"},{"numValue":66.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv"],"id":23968,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23969,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,808 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 7,336 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:S38D | null | null | null | -0.22 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":25589,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25590,"numValue":-0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25591,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,809 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 8,063 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 40.9 | KCl | 200 mM | 2LZM_A:S38D | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27441,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27442,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,810 | train | mutant | 527 | 41 | 578 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D | S38D | 1 | 1 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 12,605 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:S38D | null | null | null | 1.2 | null | null | null | 5.6 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["SAAFEC_S1262.csv"],"id":45718,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45719,"numValue":5.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45720,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,811 | train | mutant | 902 | 41 | 1,019 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38A | S38A | 1 | 1 | 0 | 0 | 38 | S | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 1,603 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:S38A | 51.45 | -1.95 | null | null | null | 1.8 | 118 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":5894,"numValue":51.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5895,"numValue":-1.95,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5896,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":5897,"numValue":118.0,"references":[],... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,812 | train | mutant | 902 | 41 | 1,019 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38A | S38A | 1 | 1 | 0 | 0 | 38 | S | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38 | A | L | false | false | 49.386572 | 32.060833 | 7,348 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:S38A | null | null | null | 0.77 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|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 | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":25620,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25621,"numValue":0.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25622,"numValue":null,"references":[],"strValue":"yes(>90%... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,813 | train | mutant | 6,772 | 41 | 7,414 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|N144D | S38D|N144D | 2 | 2 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|144 | A | L|H | false | false | 75.595743 | 25.760104 | 14,558 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S38D 2LZM_A:N144D | 54.77 | 1.35 | null | null | null | 1.8 | 119 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53814,"numValue":54.77,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53815,"numValue":1.35,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53816,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53817,"numValue":119.0,"references":... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1814 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,814 | train | mutant | 6,772 | 41 | 7,414 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|N144D | S38D|N144D | 2 | 2 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|144 | A | L|H | false | false | 75.595743 | 25.760104 | 14,565 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S38D 2LZM_A:N144D | 68.87 | 2.36 | null | null | null | 2.5 | 136 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53849,"numValue":68.87,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53850,"numValue":2.36,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53851,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53852,"numValue":136.0,"references":... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,816 | train | mutant | 6,772 | 41 | 7,414 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|N144D | S38D|N144D | 2 | 2 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|144 | A | L|H | false | false | 75.595743 | 25.760104 | 14,977 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:S38D 2LZM_A:N144D | null | null | null | -0.6 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55129,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55130,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55131,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,817 | train | mutant | 6,773 | 41 | 7,415 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D | S38D|A82P|N144D | 3 | 3 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|82|144 | A | L|T|H | false | false | 80.06005 | 25.634736 | 14,559 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | 56 | 2.58 | null | null | null | 1.8 | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53819,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53820,"numValue":2.58,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53821,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53822,"numValue":123.0,"references":[... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:1818 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,818 | train | mutant | 6,773 | 41 | 7,415 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D | S38D|A82P|N144D | 3 | 3 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|82|144 | A | L|T|H | false | false | 80.06005 | 25.634736 | 14,566 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | 70.26 | 3.75 | null | null | null | 2.5 | 138 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53854,"numValue":70.26,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53855,"numValue":3.75,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53856,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53857,"numValue":138.0,"references":... | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:1819 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,819 | train | mutant | 6,773 | 41 | 7,415 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D | S38D|A82P|N144D | 3 | 3 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|82|144 | A | L|T|H | false | false | 80.06005 | 25.634736 | 14,897 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | null | null | null | -1.59 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54931,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54932,"numValue":-1.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54933,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:1820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,820 | train | mutant | 6,773 | 41 | 7,415 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D | S38D|A82P|N144D | 3 | 3 | 0 | 0 | 38 | S | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 38|82|144 | A | L|T|H | false | false | 80.06005 | 25.634736 | 14,978 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | null | null | null | -1.05 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55132,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55133,"numValue":-1.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55134,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6935,"numValue":6.0,"position":144,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:1821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,821 | train | mutant | 1,541 | 41 | 1,738 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L39A | L39A | 1 | 1 | 0 | 0 | 39 | L | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 39 | A | H | false | false | 78.819171 | 29.7275 | 2,921 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | null | NaCl | 0.1 M | 2LZM_A:L39A | 62.7 | -2.5 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10591,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":10592,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"... | [{"id":6830,"numValue":5.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1822 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,822 | train | mutant | 1,541 | 41 | 1,738 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L39A | L39A | 1 | 1 | 0 | 0 | 39 | L | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 39 | A | H | false | false | 78.819171 | 29.7275 | 7,413 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | 53 | NaCl | 0.1 M | 2LZM_A:L39A | null | null | null | 0.9 | null | 4.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"B... | [{"datasets":[],"id":25788,"numValue":4.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25789,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25790,"numV... | [{"id":6830,"numValue":5.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1823 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,823 | train | mutant | 1,599 | 41 | 1,799 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L39P | L39P | 1 | 1 | 0 | 0 | 39 | L | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 39 | A | H | false | false | 78.819171 | 29.7275 | 2,998 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:L39P | 36.4 | -5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:L39P","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10885,"numValue":36.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10886,"numValue":-5.5,"references":[],"strValue":nul... | [{"id":6830,"numValue":5.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,824 | train | mutant | 1,599 | 41 | 1,799 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L39P | L39P | 1 | 1 | 0 | 0 | 39 | L | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 39 | A | H | false | false | 78.819171 | 29.7275 | 4,655 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:L39P | 36.4 | -5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:L39P","typ... | [{"datasets":[],"id":17212,"numValue":36.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17213,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17214,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[]... | [{"id":6830,"numValue":5.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1825 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,825 | train | mutant | 1,599 | 41 | 1,799 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L39P | L39P | 1 | 1 | 0 | 0 | 39 | L | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 39 | A | H | false | false | 78.819171 | 29.7275 | 13,900 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:L39P | null | null | 15.4 | null | null | null | null | 2.87 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51441,"numValue":15.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51442,"numValue":2.87,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51443,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51444,"numValue":null,"references":[... | [{"id":6830,"numValue":5.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,826 | train | mutant | 88 | 41 | 98 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A | N40A | 1 | 1 | 0 | 0 | 40 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 147 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:N40A | 52.75 | 1.2 | null | null | null | null | 117 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":576,"numValue":52.75,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":577,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":578,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id"... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,827 | train | mutant | 88 | 41 | 98 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A | N40A | 1 | 1 | 0 | 0 | 40 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 154 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:N40A | 63.08 | 0.88 | null | null | null | null | 125 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":604,"numValue":63.08,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":605,"numValue":0.88,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":606,"numValue":125.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1828 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,828 | train | mutant | 88 | 41 | 98 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A | N40A | 1 | 1 | 0 | 0 | 40 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 2,922 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | null | NaCl | 0.1 M | 2LZM_A:N40A | 66.1 | 0.9 | null | null | null | null | 135 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":10595,"numValue":66.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":10596,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUT... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1829 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,829 | train | mutant | 88 | 41 | 98 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A | N40A | 1 | 1 | 0 | 0 | 40 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 7,067 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:N40A | null | null | null | -0.32 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24808,"numValue":-0.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24809,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1830 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,830 | train | mutant | 88 | 41 | 98 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A | N40A | 1 | 1 | 0 | 0 | 40 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 7,414 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | 53 | NaCl | 0.1 M | 2LZM_A:N40A | null | null | null | -0.2 | null | 4.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"B... | [{"datasets":[],"id":25791,"numValue":4.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25792,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25793,"numValue":null,"references":[],"strValue":"Unknown","type":"... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1831 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,831 | train | mutant | 88 | 41 | 98 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A | N40A | 1 | 1 | 0 | 0 | 40 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 7,542 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:N40A | null | null | null | -0.43 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv"],"id":26115,"numValue":-0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26116,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,832 | train | mutant | 98 | 41 | 108 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40D | N40D | 1 | 1 | 0 | 0 | 40 | N | D | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 192 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:N40D | 66.29 | 1.14 | null | null | null | 3.5 | 132 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":787,"numValue":66.29,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":788,"numValue":1.14,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":789,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["AUTOMUT... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1833 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,833 | train | mutant | 98 | 41 | 108 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40D | N40D | 1 | 1 | 0 | 0 | 40 | N | D | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 204 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:N40D | 63.47 | 1.28 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":["HotMuSiC_S1626.csv"],"id":844,"numValue":63.47,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":845,"numValue":1.28,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":846,"numValue":3.5,"references":[],"strValue"... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1834 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,834 | train | mutant | 98 | 41 | 108 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40D | N40D | 1 | 1 | 0 | 0 | 40 | N | D | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 40 | A | H | true | false | 113.769878 | 47.08 | 6,821 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:N40D | null | null | null | -0.44 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24162,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24163,"numValue":-0.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24164,"nu... | [{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1835 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,835 | train | mutant | 7,395 | 41 | 8,078 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A|S44A|E45A|D47A|K48A|D127A|E128A|V131A|N132A | N40A|S44A|E45A|D47A|K48A|D127A|E128A|V131A|N132A | 9 | 9 | 0 | 0 | 40 | N | A | 2 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 40|44|45|47|48|127|128|131|132 | A | H | true | true | 82.368783 | 27.015431 | 15,789 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | 56.9 | 5.2 | null | null | null | 1.8 | 117 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57973,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57974,"numValue":5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57975,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57976,"numValue":117.0,"references":[]... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,836 | train | mutant | 7,395 | 41 | 8,078 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N40A|S44A|E45A|D47A|K48A|D127A|E128A|V131A|N132A | N40A|S44A|E45A|D47A|K48A|D127A|E128A|V131A|N132A | 9 | 9 | 0 | 0 | 40 | N | A | 2 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 40|44|45|47|48|127|128|131|132 | A | H | true | true | 82.368783 | 27.015431 | 16,786 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 51.7 | KCl | 25.0 mM | 2LZM_A:N40A 2LZM_A:S44A 2LZM_A:E45A 2LZM_A:D47A 2LZM_A:K48A 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -1.75 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61693,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61694,"numValue":-1.75,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61695,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6831,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,837 | train | mutant | 99 | 41 | 109 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41D | A41D | 1 | 1 | 0 | 0 | 41 | A | D | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 193 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:A41D | 65.86 | 0.71 | null | null | null | 3.5 | 138 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":792,"numValue":65.86,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":793,"numValue":0.71,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":794,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":7... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,838 | train | mutant | 99 | 41 | 109 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41D | A41D | 1 | 1 | 0 | 0 | 41 | A | D | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 205 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:A41D | 63.29 | 1.1 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":848,"numValue":63.29,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":849,"numValue":1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":850,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":85... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,839 | train | mutant | 99 | 41 | 109 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41D | A41D | 1 | 1 | 0 | 0 | 41 | A | D | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 6,822 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:A41D | null | null | null | -0.29 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | METHOD|PH|EXP_TEMPERATURE|MEASURE|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":24165,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24166,"numValue":-0.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24167,"numValue":null,"referenc... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,840 | train | mutant | 229 | 41 | 259 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41S | A41S | 1 | 1 | 0 | 0 | 41 | A | S | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 415 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A41S | 49.78 | -1.77 | null | null | null | null | 106 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1711,"numValue":49.78,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1712,"numValue":-1.77,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1713,"numValue":106.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,841 | train | mutant | 229 | 41 | 259 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41S | A41S | 1 | 1 | 0 | 0 | 41 | A | S | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 7,584 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A41S | null | null | null | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26225,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26226,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,842 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 904 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:A41V | 54.52 | 1.1 | null | null | null | 1.8 | 132 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3351,"numValue":54.52,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3352,"numValue":1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3353,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,843 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 911 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:A41V | 67.21 | 0.7 | null | null | null | 2.5 | 141 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3386,"numValue":67.21,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3387,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3388,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,844 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 995 | ProTherm | 2.03 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A41V | 43.07 | 1.6 | null | null | null | null | 83.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":3729,"numValue":43.07,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3730,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3731,"numValue":83.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,845 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 998 | ProTherm | 2.83 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A41V | 52.43 | 1.33 | null | null | null | null | 109.7 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":3741,"numValue":52.43,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3742,"numValue":1.33,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3743,"numValue":109.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,846 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 6,726 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:A41V | null | null | null | -0.3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23900,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23901,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23902,"numValue":null,"reference... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,847 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 7,341 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:A41V | null | null | null | -0.41 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":25604,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25605,"numValue":-0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25606,"numValue":null,"references":[],"strValue":"Unknown","typ... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1848 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,848 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 7,613 | ProTherm | 2.83 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 51.1 | KCl | 0.2 M | 2LZM_A:A41V | null | null | null | -0.45 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":51.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M",... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26291,"numValue":-0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26292,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,849 | train | mutant | 529 | 41 | 580 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A41V | A41V | 1 | 1 | 0 | 0 | 41 | A | V | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41 | A | H | false | false | 38.739844 | 27.767 | 8,054 | ProTherm | 2.03 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 41.47 | KCl | 0.2 M | 2LZM_A:A41V | null | null | null | -0.42 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":41.47,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M"... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27423,"numValue":-0.42,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27424,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,850 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 14,557 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:A41V 2LZM_A:V131A | 55.25 | 1.83 | null | null | null | 1.8 | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53809,"numValue":55.25,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53810,"numValue":1.83,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53811,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53812,"numValue":123.0,"references":... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1851 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,851 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 14,564 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:A41V 2LZM_A:V131A | 68.02 | 1.51 | null | null | null | 2.5 | 140 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53844,"numValue":68.02,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53845,"numValue":1.51,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53846,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53847,"numValue":140.0,"references":... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,852 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 14,580 | ProTherm | 2.03 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A41V 2LZM_A:V131A | 43.67 | 2.2 | null | null | null | null | 80.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53919,"numValue":43.67,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53920,"numValue":2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53921,"numValue":80.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53922,"numValue":null,"references":... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1853 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,853 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 14,581 | ProTherm | 2.83 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:A41V 2LZM_A:V131A | 52.91 | 1.81 | null | null | null | null | 107.3 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53923,"numValue":52.91,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53924,"numValue":1.81,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53925,"numValue":107.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53926,"numValue":null,"references... | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,854 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 14,895 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:A41V 2LZM_A:V131A | null | null | null | -0.66 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54925,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54926,"numValue":-0.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54927,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,855 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 14,976 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:A41V 2LZM_A:V131A | null | null | null | -0.76 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55126,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55127,"numValue":-0.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55128,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,856 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 15,032 | ProTherm | 2.83 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 51.1 | KCl | 0.2 M | 2LZM_A:A41V 2LZM_A:V131A | null | null | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":51.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M",... | [{"datasets":[],"id":55253,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55254,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,857 | train | mutant | 6,771 | 41 | 7,413 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | V131A|A41V | V131A|A41V | 2 | 2 | 0 | 0 | 131 | V | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 41|131 | A | H | true | false | 66.643874 | 23.664572 | 15,097 | ProTherm | 2.03 | CD | Thermal | K2HPO4, NaH2PO4 | 1.05 M, 1.26 M | 41.47 | KCl | 0.2 M | 2LZM_A:A41V 2LZM_A:V131A | null | null | null | -0.56 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 103 | ARTICLE | A mutant T4 lysozyme (Val 131----Ala) designed to increase thermostability by the reduction of strain within an alpha-helix. | 1,990 | 10.1002/prot.340070208 | 2326253 | Proteins;7;198-204 | 3 | Baase W A|Matthews B W|Dao-Pin S | [{"numValue":2.03,"strValue":null,"type":"PH"},{"numValue":41.47,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"K2HPO4, NaH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"1.05 M, 1.26 M"... | [{"datasets":[],"id":55409,"numValue":-0.56,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55410,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1858 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,858 | train | mutant | 230 | 41 | 260 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42S | A42S | 1 | 1 | 0 | 0 | 42 | A | S | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 416 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A42S | 44.06 | -7.49 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1715,"numValue":44.06,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1716,"numValue":-7.49,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1717,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,859 | train | mutant | 230 | 41 | 260 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42S | A42S | 1 | 1 | 0 | 0 | 42 | A | S | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 7,585 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A42S | null | null | null | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26227,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26228,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,860 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 2,923 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | null | NaCl | 0.1 M | 2LZM_A:A42K | 54.2 | -11 | null | null | null | null | 64 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10599,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10600,"numValue":-11.0,"references":[],"strValue":nu... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,861 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,064 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 38.8 | -15.3 | null | null | 71.94 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15014,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15015,"numValue":-15.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15016,"numValue":71.94,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1862 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,862 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,065 | ProTherm | 3.2 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 43.1 | null | null | null | 79.11 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15018,"numValue":43.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15019,"numValue":79.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15020,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,863 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,066 | ProTherm | 3.3 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 44.9 | -14.5 | null | null | 84.61 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15021,"numValue":44.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15022,"numValue":-14.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15023,"numValue":84.61,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,864 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,067 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 47.9 | -14.2 | null | null | 91.54 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15025,"numValue":47.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15026,"numValue":-14.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15027,"numValue":91.54,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,865 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,068 | ProTherm | 3.6 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 50.1 | null | null | null | 88.91 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15029,"numValue":50.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15030,"numValue":88.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15031,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,866 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,069 | ProTherm | 3.7 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 51.4 | -13.2 | null | null | 97.75 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15032,"numValue":51.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15033,"numValue":-13.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15034,"numValue":97.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,867 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 4,070 | ProTherm | 4 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:A42K | 54.4 | null | null | null | 105.16 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:A42K","type":"... | [{"datasets":[],"id":15036,"numValue":54.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15037,"numValue":105.16,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15038,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,868 | train | mutant | 1,542 | 41 | 1,739 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42K | A42K | 1 | 1 | 0 | 0 | 42 | A | K | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 7,415 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | 53 | NaCl | 0.1 M | 2LZM_A:A42K | null | null | null | 3.7 | null | 4.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"B... | [{"datasets":[],"id":25794,"numValue":4.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25795,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25796,"numValue":null,"references... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1869 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,869 | train | mutant | 1,956 | 41 | 2,186 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42V | A42V | 1 | 1 | 0 | 0 | 42 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 3,773 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A42V | 44.2 | -7.5 | null | null | null | null | 79 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13926,"numValue":44.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13927,"numValue":-7.5,"references":[],"strValue":null,"type":"DTM"},{"dat... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,871 | train | mutant | 1,958 | 41 | 2,188 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42I | A42I | 1 | 1 | 0 | 0 | 42 | A | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 3,775 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A42I | 42.8 | -8.9 | null | null | null | null | 67 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13934,"numValue":42.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":13935,"numValue":-8.9,"references":[],"strValue":null... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1872 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,872 | train | mutant | 1,959 | 41 | 2,189 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42F | A42F | 1 | 1 | 0 | 0 | 42 | A | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 3,776 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A42F | 40.5 | -11.2 | null | null | null | null | 56 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13938,"numValue":40.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":13939,"numValue":-11.2,"references":[],"strValue":null,"type":"DTM"}... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,873 | train | mutant | 4,335 | 41 | 4,844 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A42G | A42G | 1 | 1 | 0 | 0 | 42 | A | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 42 | A | H | false | false | 0 | 25.899 | 10,021 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:A42G | null | null | 11.7 | 3.2 | null | null | null | null | 2.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 664 | ARTICLE | Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. | 2,007 | 10.1110/ps.062632807 | 17400925 | Protein Sci;16;852-62 | 3 | Marqusee Susan|Cellitti Jason|Bernstein Rachel | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"B... | [{"datasets":[],"id":34421,"numValue":11.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34422,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34423,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34424,"numValue":null,... | [{"id":6833,"numValue":8.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,874 | train | mutant | 89 | 41 | 99 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K43A | K43A | 1 | 1 | 0 | 0 | 43 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 43 | A | H | true | false | 50.074322 | 37.580556 | 148 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:K43A | 48.7 | -2.95 | null | null | null | null | 101 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":580,"numValue":48.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":581,"numValue":-2.95,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":582,"numValue":101.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6834,"numValue":5.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,875 | train | mutant | 89 | 41 | 99 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K43A | K43A | 1 | 1 | 0 | 0 | 43 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 43 | A | H | true | false | 50.074322 | 37.580556 | 155 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:K43A | 59.12 | -3.08 | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":608,"numValue":59.12,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":609,"numValue":-3.08,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":610,"numValue":108.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6834,"numValue":5.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,876 | train | mutant | 89 | 41 | 99 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K43A | K43A | 1 | 1 | 0 | 0 | 43 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 43 | A | H | true | false | 50.074322 | 37.580556 | 2,924 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | null | NaCl | 0.1 M | 2LZM_A:K43A | 62.1 | -3.1 | null | null | null | null | 124 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10603,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":10604,"numValue":-3.1,"references":[],"strValue":nul... | [{"id":6834,"numValue":5.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,877 | train | mutant | 89 | 41 | 99 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K43A | K43A | 1 | 1 | 0 | 0 | 43 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 43 | A | H | true | false | 50.074322 | 37.580556 | 7,068 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:K43A | null | null | null | 1.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24810,"numValue":1.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24811,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6834,"numValue":5.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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